The Cystic Fibrosis Story / CFTR
Research, not medical advice
CFTR is a human protein, and variants of it are linked to cystic fibrosis. Here are four published structures of it, each drawn as a smooth tube through the position of one atom in every amino acid it places. Turn them, switch between them, and see where amino acid 508 sits, and where it is absent in the two structures of CFTR with F508del (8EIQ and 8EJ1).
Primary Sources: RCSB PDB entries 6MSM, 5UAK, 8EIQ, 8EJ1 and UniProt P13569 (Zhang & Chen Cell 2017/2018; Fiedorczuk & Chen Nature 2022).
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GitHub Proof: cf-research/tools/cftr-model ↗ · data/cftr.lock.json ↗
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Structure
Colors
Tools for reading the four structures. They run in your browser on the files described further down this page; nothing is sent anywhere.
Simulating allosteric corrector rescue and nonsense readthrough kinetics for Class I mutations (G542X and W1282X) alongside Cryo-EM 3D coordinates: SMG1-mediated transcript rescue, engineered suppressor tRNA opal readthrough, and ERAD escape curves.
Exon 12 · UGA G (+4 flanking context)
541 aa translated (missing 939 aa) · Ribosome Quality Control (RQC) & Proteasomal Cleavage
Δd(6MSM→5UAK) = 8.52 Å · Δd(6MSM→8EIQ) = 1.93 Å
Aborts at residue 541 before NBD1 alpha-core; correctors cannot bind without prior readthrough (cotranslational RQC clearance).
Investigational biophysical model based on PDB 6MSM/8EIQ Cryo-EM coordinates, RefSeq NM_000492.4, and Manfredi et al. (Biochemistry 2025). Research simulation only; not clinical guidance.
Compare normal apical membrane trafficking, PKA phosphorylation, and ATP-dependent chloride conductance against F508del domain misfolding and endoplasmic reticulum-associated degradation (ERAD).
Biophysical channel gating & trafficking comparison: apical ion transport versus ubiquitin-proteasome degradation. Schematic, not a structure.
In-silico biophysical feasibility modeling for prime editing pegRNA primer binding site (PBS) thermodynamics, reverse transcriptase template (RTT) length constraints, PE3/PE3b nicking strategies, and dual-vector delivery packaging limits.
Biophysical prime editing flap resolution & delivery packaging model: in-silico pegRNA thermodynamics and dual-vector constraints. Schematic, not a structure.
Differential scanning calorimetry (DSC) unfolding transitions, ΔΔG coupling with ICL4, and corrector rescue energetics grounded in PDB 6MSM and 8EIQ.
Research, not medical advice. Computational biophysical model based on DSC melting profiles and structural interfaces (PDB 6MSM, 8EIQ). NCT04043806, NCT06468527. Schematic, not a structure.
Monod-Wyman-Changeux (MWC) 2N microstate grand partition function coupling Cryo-EM pockets TMD1 (VX-661), TMD2 (VX-445 / VX-121), and the TM4/5/8 lipid-facing gating hinge (VX-770 / VX-561) in PDB 8EIQ and 6MSM.
Research, not medical advice. Computational biophysical model based on MWC grand partition functions and Cryo-EM coordinates (PDB 8EIQ, 6MSM; Fiedorczuk & Chen, Science 2022, DOI 10.1126/science.ade2216). ClinicalTrials.gov data (NCT04043806, NCT06468527) are used with attribution to the U.S. National Library of Medicine (NLM). Schematic, not a structure.
In plain words: Some CFTR mutations leave the channel trapped shut like a stiff spring. Potentiators wedge into the channel to hold it open longer. When two different potentiators bind at once, their combined grip can release trapped channels far more than either medicine acting alone.
Thermodynamic mutant cycle analysis and free-energy coupling (ΔΔGopen = -RT ln(Keq / Keq,0)) between TM8 lipid-hinge potentiators (Ivacaftor / Deutivacaftor) and NBD-TMD interface boosters (GLPG1837) across Class III (G551D, G1244E, S549N) and Class IV (R117H) gating alleles.
Research, not medical advice. Computational thermodynamic mutant cycle model grounded in human Cryo-EM coordinates (PDB 8EIQ, 8EJ1, 6MSM; Van Goor et al., PNAS 2009, DOI 10.1073/pnas.0904709106; Liu et al., Science 2019, DOI 10.1126/science.aaw7611; Yeh et al., J Gen Physiol 2020, DOI 10.1085/jgp.202012676; Zhang et al., Cell 2021, DOI 10.1016/j.cell.2021.02.012). ClinicalTrials.gov data (NCT00909532) are cited with attribution to the U.S. National Library of Medicine (NLM): ClinicalTrials.gov does not evaluate safety or efficacy; listing on the registry does not denote government endorsement. Schematic, not a structure.
Visualizing 3D Cα residue backbone truncation, steric residue loss, and thermal unfolding profiles for W1282X, G542X, and R1162X grounded in human Cryo-EM coordinates (PDB 6MSM, 5UAK, 8EIQ).
Research, not medical advice. Computational structural analysis grounded in human CFTR Cryo-EM coordinates (PDB 6MSM, 5UAK, 8EIQ), NCT04135495, and Manfredi et al. (Biochemistry 2025, DOI: 10.1021/acs.biochem.5c00590). Schematic, not a structure.
Exploring RefSeq NM_000492.4 protospacer windows (SpCas9 / SpG / SpRY), ABE8e bystander deamination, cryptic splice ASO thermodynamics, and ESM-2 / ThermoMPNN zero-shot biophysical disentanglement across CFTR mutation classes.
Sequence-guided therapeutic modality
Catalytic window or folding shift
Off-target collision or mechanistic phenotype
TLR9 CpG dinucleotides or Band C Golgi export
Research, not medical advice. Computational model based on RefSeq NM_000492.4, ESM-2 (Lin et al., Science 2023, DOI 10.1126/science.ade2574), ProteinMPNN (Dauparas et al., Science 2022, DOI 10.1126/science.add2187), and Cryo-EM coordinates (PDB 5UAK, 6MSM, 8EIQ). ClinicalTrials.gov data (NCT05248230, NCT05668741, NCT04684641, NCT04135495) are used with attribution to the U.S. National Library of Medicine (NLM); ClinicalTrials.gov does not evaluate safety or efficacy. The lab does not assess efficacy or recommend treatments. Schematic, not a structure.
Evaluating SpliceAI and Evo-2 cryptic splice donor/acceptor activation, in-frame pseudoexon inclusion, and steric-blocking antisense oligonucleotide (ASO) rescue kinetics across non-coding CFTR alleles.
Splice site gain/loss and pathogenicity
Thermodynamic ΔG°, Tm, and estimated EC50
Normal mature mRNA restoration
Electrophysiological function vs curative threshold
Research, not medical advice. Computational model based on SpliceAI (Jaganathan et al., Cell 2019, DOI 10.1016/j.cell.2018.12.015), Evo 2 (Brixi et al., bioRxiv 2025, DOI 10.1101/2025.02.18.638918), and ASO steric blocking kinetics (Oren et al., J Cyst Fibros 2022, DOI 10.1016/j.jcf.2021.08.014). ClinicalTrials.gov data (NCT06429176, NCT04684641) are used with attribution to the U.S. National Library of Medicine (NLM); ClinicalTrials.gov does not evaluate safety or efficacy. The lab does not assess efficacy or recommend treatments. Cryo-EM structural accessions: PDB 6FF4, 7ABI, 6MSM. Schematic, not a structure.
In plain words: Deep intronic CFTR mutations create false splice sites that recruit the human U1 snRNP complex and insert faulty protein-truncating sequences. Synthetic decoy oligonucleotides (like inhaled SPL84) compete for these cryptic sites, kicking off U1 snRNP and restoring healthy, full-length CFTR protein.
Modeling SantaLucia nearest-neighbor base-pairing thermodynamics, competitive mass-action displacement, and pseudoexon exclusion dose-response curves across deep-intronic CFTR mutations (3849+10kb C->T and 1811+1.6kb A->G).
Research, not medical advice. Grounded in Scalet et al. (Am J Hum Genet 2019, DOI: 10.1093/hmg/dds045), Rogalska et al. (Nucleic Acids Res 2019, DOI: 10.1002/humu.22931), Kim et al. (Am J Hum Genet 2019, DOI: 10.1016/j.ajhg.2019.09.011), and Sharma et al. (Sci Rep 2020, DOI: 10.1038/s41598-020-65842-8). Structural pre-spliceosome coordinates: RCSB PDB 6QX9 (3.3 Å). Clinical surveillance: ClinicalTrials.gov NCT06429176 (SPL84 Phase 1/2). ClinicalTrials.gov does not evaluate safety or efficacy; listing on the registry does not denote government endorsement.
In plain words: Guanine-rich stretches in the CFTR promoter, 5' UTR, and coding region fold into four-stranded knots called G-quadruplexes (G4). In the right spots, these act like speed bumps that let the cell fold CFTR properly; when over-stabilized by small-molecule ligands, they can jam ribosomes and lower CFTR protein output.
Modeling G-quartet stacking thermodynamics, monovalent cation coordination (K+ vs Na+), small-molecule stabilization (Pyridostatin / PDS, TMPyP4), and DHX36/RHAU helicase unwinding kinetics across human CFTR (NM_000492.4).
Research, not medical advice. Grounded in Haensel-Hertsch et al. (Nucleic Acids Res 2017, DOI: 10.1093/nar/gkw1157), Mori et al. (J Med Chem 2020, DOI: 10.1021/acs.jmedchem.0c00827), Kwok et al. (Nat Methods 2016, DOI: 10.1038/nmeth.3965), and Endoh & Sugimoto (Biopolymers 2016, DOI: 10.1002/wrna.1158). Clinical surveillance: ClinicalTrials.gov NCT05668741 (BEACON-CF). ClinicalTrials.gov does not evaluate safety or efficacy; listing on the registry does not denote government endorsement. Coordinates: RCSB PDB 6MSM, 8EIQ, 8EJ1.
In plain words: UniProt P13569 catalogs 209 natural human CFTR variants across all 27 exons of RefSeq NM_000492.4. When superposed onto four published Cryo-EM structures (6MSM, 5UAK, 8EIQ, 8EJ1), 191 variants sit at resolved 3D alpha-carbon coordinates while 18 fall inside unplaced disordered regions (such as the R-domain) and 17 lie within 3 codons of an exon-intron splice boundary.
Deterministic coordinate mapping across 209 UniProt P13569 natural variants (CC BY 4.0) and 17 ClinVar/MyVariant predictor benchmark records: Horn’s quaternion C-alpha displacements (6MSM vs 5UAK and 8EIQ), Euclidean distance to F508, 27-exon splice proximity, and sequence vs structure predictor discordance (VF-1 to VF-4).
| Variant | Residue | Exon (NM_000492.4) | Domain | PDB Placed | ΔCα (6MSM vs 5UAK) | Dist to F508 (6MSM) |
|---|
Research, not medical advice. Schematic, not a structure. Grounded in UniProtKB P13569 (entry version 286, CC BY 4.0, redistribute: true), RefSeq NM_000492.4 (27 exons), and RCSB PDB Cryo-EM entries 6MSM, 5UAK, 8EIQ, and 8EJ1 (CC0 1.0, redistribute: true; Zhang & Chen Cell 2017 / PNAS 2018; Fiedorczuk & Chen Science 2022). CFTR2 and CFTR-France variant tables are never redistributed (redistribute: false in sources/catalog.yaml). Open-access JSON: Download cftr_variant_domain_benchmark.json (v2.0.0).
Reconciles canonical RefSeq (NM_000492.4), protein HGVS (NP_000483.3), Ensembl (ENST00000003084), 0-based NCBI SPDI (NC_000007.14), and UniProtKB P13569 / PDB 6MSM structural domains alongside jurisdictionally separated US FDA SPL and UK MHRA regulatory context.
Research, not medical advice. Coordinate normalization and regulatory tables never determine individual clinical eligibility; consult a licensed CF care team and genetic counselor. Grounded in Sosnay et al. (Nat Genet 2013, DOI: 10.1038/ng.2745), Veit et al. (Mol Biol Cell 2016, DOI: 10.1091/mbc.e14-04-0935), Holmes et al. (Bioinformatics 2020, DOI: 10.1093/bioinformatics/btz856), Middleton et al. (N Engl J Med 2019, DOI: 10.1056/NEJMoa1908639), PDB 6MSM & 5UAK, and ClinicalTrials.gov NCT05248230, NCT05668741, NCT05033080. ClinicalTrials.gov does not evaluate safety or efficacy; listing on the registry does not denote government endorsement.
In plain words: While approved CFTR modulators help approximately 85–90% of people with cystic fibrosis, roughly 10–15% carry Class I nonsense or frameshift mutations (such as G542X, W1282X, R553X, and 3849+10kbC->T) that produce little or no full-length protein. This census cross-references 209 CFTR2 variants against 54,043 patients in the European registry (ECFSPR) and 79 active/recruiting trials to spotlight the 5 recruiting trials specifically pursuing curative genetic correction for these non-responsive alleles.
Cross-scale synthesis linking 209 natural CFTR variants to 4 Cryo-EM atomic structures (6MSM active dephosphorylated, 5UAK inactive, 8EIQ modulator-bound, 8EJ1 G551D gating), ECFSPR cohort prevalence, and 5/57 recruiting clinical trials targeting non-responsive Class I/VII mutations.
| Variant | Class | cDNA Notation | Exon / Domain | PDB Structures | ECFSPR Cohort | Curative Clinical Trials |
|---|
Research, not medical advice. Independent research from Sensei Ewok CF Lab; not clinical guidance. Structural coordinates from RCSB PDB (6MSM, 5UAK, 8EIQ, 8EJ1). Clinical trial surveillance from ClinicalTrials.gov (NCT05248230, NCT05668741, NCT04135495, NCT06429176). ClinicalTrials.gov does not evaluate safety or efficacy; listing on the registry does not denote government endorsement. Epidemiological cohort from ECFSPR 2026 Annual Report (54,043 patients).
In plain language: Rectal organoids (“mini-guts” grown from patient stem cells) preserve a person’s exact CFTR variants. Forskolin stimulates cAMP-dependent channel opening, driving fluid into the lumen and swelling the organoid if CFTR functions. Measuring surface area expansion (ΔAUC120) in vitro quantifies drug response and predicts in vivo improvements in sweat chloride and lung function.
Schematic lumen expansion driven by CFTR chloride and fluid secretion (Dekkers et al., Nat Med 2013).
Intermediate swelling crossing the 1,000 AUC clinical threshold. Personalized evaluation under N-of-1 trial protocols (such as HIT-CF Europe NCT06468527) is indicated.
In vitro research surrogate assay, not medical advice. Rectal organoid swelling provides preclinical theratyping evidence and does not denote in vivo clinical efficacy or regulatory approval. Individual patient pharmacokinetics, lung tissue penetration, and cellular adherence vary. Clinical trial protocol listing (HIT-CF Europe NCT06468527) does not denote government endorsement.
In plain words: The CFTR protein contains 12 membrane-spanning helices (TM1–TM12) that weave through the cell’s fatty outer membrane to form an open chloride pore. In healthy cells, these helices naturally partition into the lipid bilayer according to their thermodynamic water-to-lipid transfer free energies. However, TM8 contains an unwound polar segment that makes it thermodynamically unstable on its own. Small-molecule correctors—like tezacaftor (VX-661) and elexacaftor (VX-445) in Trikafta—act as molecular splints that bind hydrophobic pockets in the transmembrane domains, remodeling the lipid shell and lowering the insertion free energy by more than 3.5 kcal/mol. This stabilizes fragile mutant proteins (like L206W and V232D) against premature degradation so they can mature and reach the cell surface. This is research, not medical advice.
Quantitative biophysical thermodynamic simulation of Wimley-White water-to-POPC transfer free energies across TM1–TM12 in dephosphorylated (PDB 6MSM) versus phosphorylated active (PDB 5UAK) conformations, mattress-model hydrophobic thickness mismatch (ER 27.5 Å vs apical PM 31.8 Å), allosteric corrector lipid-shell stabilization, and Boltzmann quality-control rescue of rare transmembrane missense variants.
Primary Evidence & Structural Registry Anchors:
Each step sets the picture above. The words stay here whether or not the picture runs.
This is human CFTR, drawn as one point for each amino acid the model places, joined in order. The positions come from a model that scientists fitted to electron-microscope data (structure 6MSM, published in 2018). Drag to turn it, or use the sliders.
CFTR is a single chain of 1,480 amino acids. UniProt marks two membrane-spanning parts (residues 81 to 365 and 859 to 1155) and two nucleotide-binding parts (423 to 646 and 1210 to 1443). It marks the long stretch from 654 to 831 as disordered, and none of that stretch is placed in the chain this page draws, in any of the four files. Three of the files (6MSM, 5UAK and 8EIQ) also hold a short separate fragment of 16 to 19 residues of unknown identity, whose place in the sequence is not assigned; 5UAK's file calls it the R domain. It is not drawn. Wherever a model leaves out a stretch, a dotted line shows only that it is not drawn.
Residue 508 sits inside the first nucleotide-binding part. In structure 6MSM it is phenylalanine, one of the amino acids that make up proteins. The rose ring and dot show it.
Structure 8EIQ is human CFTR carrying F508del, the loss of the amino acid at position 508. Its model runs from residue 507 straight to 509, and the empty ring marks the place midway between them. Its file also records an engineered change at position 1371 (glutamate replaced by glutamine), as do the files for 6MSM and 8EJ1; 5UAK does not have it. This structure was solved with the three medicines of Trikafta (the title in its file lists them) and with ATP and magnesium present. This page does not show where they sit or how they act.
Here the membrane-spanning parts of each model are lined up on 6MSM, a computation made for this page. After that fit, the membrane-spanning parts of 8EIQ are 0.84 Å from those of 6MSM, as a root-mean-square distance over 566 residues (1 Å is a ten-billionth of a meter). 5UAK and 8EJ1 are about 5 Å away (5.01 Å over 557 residues, and 4.87 Å over 547). 8EJ1 was solved at lower resolution (6.9 Å), so less detail is available for it. These numbers describe differences in shape between models. They do not say why, they do not say that any structure is open or closed, and they do not show what the medicines do.
What the published reports say about who can get CFTR modulators, and where, is on the Cystic Fibrosis Story page, with its sources.
Read straight from the structure files. The last column lists the stretches a model does not place.
| Structure | What the file calls it | Method | Residues placed | Residue 508 | Paper | Residues not placed | Differs from UniProt's sequence |
|---|---|---|---|---|---|---|---|
| 6MSM | Phosphorylated, ATP-bound human cystic fibrosis transmembrane conductance regulator (CFTR) | Electron microscopy, 3.2 Å; deposited 2018-10-16 | 1181 of 1480 | present (phenylalanine) | Proc. Natl. Acad. Sci. U.S.A. 2018, PubMed 30459277 | 410 to 434, 638 to 844, 890 to 899, 1174 to 1201, 1452 to 1480 | 1371: glutamine in the file, glutamate in UniProt (the file says: engineered mutation); 9 expression-tag residues beyond the protein, not drawn |
| 5UAK | Dephosphorylated, ATP-free human cystic fibrosis transmembrane conductance regulator (CFTR) | Electron microscopy, 3.87 Å; deposited 2016-12-19 | 1139 of 1480 | present (phenylalanine) | Cell 2017, PubMed 28340353 | 1 to 4, 403 to 438, 646 to 843, 884 to 908, 1173 to 1206, 1437 to 1480 | 9 expression-tag residues beyond the protein, not drawn |
| 8EIQ | The complex of phosphorylated human delta F508 cystic fibrosis transmembrane conductance regulator (CFTR) with Trikafta [elexacaftor (VX-445), tezacaftor (VX-661), ivacaftor (VX-770)] and ATP/Mg | Electron microscopy, 3 Å; deposited 2022-09-15 | 1162 of 1480 | absent: the chain runs from 507 to 509 | Science 2022, PubMed 36264792 | 403 to 436, 508, 637 to 845, 886 to 901, 1174 to 1202, 1452 to 1480 | 508: phenylalanine is not in the file (the file says: deletion); 1371: glutamine in the file, glutamate in UniProt (the file says: engineered mutation) |
| 8EJ1 | Dephosphorylated human delta F508 cystic fibrosis transmembrane conductance regulator (CFTR) | Electron microscopy, 6.9 Å; deposited 2022-09-16 | 1127 of 1480 | absent: the chain runs from 507 to 509 | Science 2022, PubMed 36264792 | 1 to 2, 109 to 117, 403 to 436, 508, 637 to 840, 887 to 909, 1122 to 1124, 1174 to 1206, 1437 to 1480 | 508: phenylalanine is not in the file (the file says: variant); 1371: glutamine in the file, glutamate in UniProt (the file says: engineered mutation) |
Every number on this page is read from a file or computed from one. The table says which, and how to check it.
| What | Value on this page | Where it comes from | How to check it |
|---|---|---|---|
| Residues placed | 6MSM 1181; 5UAK 1139; 8EIQ 1162; 8EJ1 1127 | The four .cif.gz files from the RCSB Protein Data Bank, chain A, model 1. | Count the ATOM lines whose atom name is CA in chain A, model 1. |
| Method, resolution, date | 6MSM 3.2 Å, deposited 2018-10-16; 5UAK 3.87 Å, deposited 2016-12-19; 8EIQ 3 Å, deposited 2022-09-15; 8EJ1 6.9 Å, deposited 2022-09-16 | Fields _exptl.method, _em_3d_reconstruction.resolution and _pdbx_database_status.recvd_initial_deposition_date in each file. | Open the file header and read those fields. |
| Paper | 6MSM Proc. Natl. Acad. Sci. U.S.A. 2018, PubMed 30459277; 5UAK Cell 2017, PubMed 28340353; 8EIQ Science 2022, PubMed 36264792; 8EJ1 Science 2022, PubMed 36264792 | Fields _citation.journal_abbrev, _citation.year and _citation.pdbx_database_id_PubMed. | Open the PubMed record. |
| Stretches not placed | listed in the table above | Computed from the residue numbers placed. | List the residue numbers that have a CA atom and take the gaps between 1 and 1480. |
| How each file differs from UniProt’s sequence | 6MSM 1371; 5UAK none; 8EIQ 508, 1371; 8EJ1 508, 1371 | The file’s own _struct_ref_seq_dif list; expression-tag residues beyond the protein are counted, not drawn. | Read that list in the file. |
| Length and part boundaries | 1,480 residues; parts 81 to 365, 423 to 646, 859 to 1155, 1210 to 1443; a region UniProt marks as disordered (the regulatory, or R, region) 654 to 831 | UniProt P13569, entry version 286, annotation updated 2026-09-02: the sequence, and the features of type Domain and Region. | Open the entry on uniprot.org. |
| Residue numbering | 4,609 placed residues checked; 3 differ from UniProt, all declared by their files | Every placed residue is compared with the amino acid UniProt has at that number; the build stops if one disagrees without its file saying so. | Run tools/cftr-model/build_traces.py (in the cf-research repository) with the downloaded files; tools/cftr-model/tests/test_data.py also checks it. |
| Distance after fitting | 6MSM the reference; 5UAK 5.01 Å over 557 residues; 8EIQ 0.84 Å over 566 residues; 8EJ1 4.87 Å over 547 residues | Computed for this page. Take the alpha carbons that 6MSM and the structure both place, with the same amino acid, inside UniProt residues 81 to 365 and 859 to 1155; fit one onto the other by a rigid rotation and shift (Horn’s method); the number is the root-mean-square distance left. | Run tools/cftr-model/build_traces.py (in the cf-research repository); tools/cftr-model/tests/test_data.py shows the fit recovers a known rotation. |
| Positions in the view | angstrom, rounded to 0.1 | The alpha-carbon coordinates after that fit, centered on the placed residues of 6MSM. | Save the CSV from the tools above. |
| Topology and helices | 12 transmembrane segments; 13 topological domains | UniProt P13569 features of type Transmembrane and Topological domain. | Open the entry on uniprot.org. |
| Variant positions | 209 entries: 196 at a single residue (165 different positions) and 13 spanning several residues | UniProt P13569 features of type Natural variant (position, residues and wording as UniProt gives them). Only single-residue entries are drawn as beads; the others are listed in the residue look-up. | Open the entry on uniprot.org. |
Structures (RCSB Protein Data Bank, archive files under CC0 1.0; please cite the entry and its paper): 6MSM: Molecular structure of the ATP-bound, phosphorylated human CFTR. Proc. Natl. Acad. Sci. U.S.A. 2018. PubMed 30459277. Entry deposited 2018-10-16. 5UAK: Molecular Structure of the Human CFTR Ion Channel. Cell 2017. PubMed 28340353. Entry deposited 2016-12-19. 8EIQ: Molecular structures reveal synergistic rescue of Delta 508 CFTR by Trikafta modulators. Science 2022. PubMed 36264792. Entry deposited 2022-09-15. 8EJ1: Molecular structures reveal synergistic rescue of Delta 508 CFTR by Trikafta modulators. Science 2022. PubMed 36264792. Entry deposited 2022-09-16. Annotations: UniProt P13569, entry version 286, annotation last updated 2026-09-02 (CC BY 4.0; how to cite UniProt: https://www.uniprot.org/help/publications). Fit and numbers on this page: computed from those files with tools/cftr-model/build_traces.py in the cf-research repository (alpha-carbon atoms of chain A, model 1).
