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Cystic Fibrosis Transmembrane Conductance Regulator: Solution Structures of Peptides Based on the Phe508 Region, the Most Common Site of Disease-Causing DeltaF508 Mutation
Authors
Massiah, M.A., Ko, Y.H., Pedersen, P.L., Mildvan, A.S.
Assembly
CYSTIC FIBROSIS TRANSMEMBRANE CONDUNTANCE REGULATOR (CFTR)
Entity
1. CYSTIC FIBROSIS TRANSMEMBRANE CONDUNTANCE REGULATOR (CFTR) (polymer, Thiol state: not present), 25 monomers, 2903.313 Da Detail

MPGTIKENII GVSYDEYRYR SVIKA


Formula weight
2903.313 Da
Source organism
Homo sapiens
Exptl. method
NMR
Refine. method
DISTANCE GEOMETRY
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 96.0 %, Completeness: 80.9 %, Completeness (bb): 94.1 % Detail

Polymer type: polypeptide(L)

Total1H
All80.9 % (127 of 157)80.9 % (127 of 157)
Backbone94.1 % (48 of 51)94.1 % (48 of 51)
Sidechain74.5 % (79 of 106)74.5 % (79 of 106)
Aromatic100.0 % (12 of 12)100.0 % (12 of 12)
Methyl85.7 % (12 of 14)85.7 % (12 of 14)

1. PROTEIN (CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR (CFTR))

MPGTIKENII GVSYDEYRYR SVIKA

Sample

Pressure 1 atm, Temperature 298 (±0.5) K, pH 4.0 (±0.1)


#NameIsotope labelingTypeConcentration
1PROTEIN (CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR (CFTR))0.0 ~ 0.0 mM
2H2O90 %
3DMSO[U-2H]10 %

Protein Blocks Logo
Calculated from 13 models in PDB: 1CKZ, Strand ID: A Detail


Release date
2000-12-03
Citation
Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation
Massiah, M.A., Ko, Y.H., Pedersen, P.L., Mildvan, A.S.
Biochemistry (1999), 38, 7453-7461, PubMed 10360942 , DOI 10.1021/bi9903603 ,
Related entities 1. CYSTIC FIBROSIS TRANSMEMBRANE CONDUNTANCE REGULATOR (CFTR), : 1 : 6 : 1 : 78 entities Detail
Interaction partners 1. CYSTIC FIBROSIS TRANSMEMBRANE CONDUNTANCE REGULATOR (CFTR), : 29 interactors Detail
Experiments performed 3 experiments Detail
nullKeywords Cystic fibrosis, peptides, NMR