1CKW

CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR: SOLUTION STRUCTURES OF PEPTIDES BASED ON THE PHE508 REGION, THE MOST COMMON SITE OF DISEASE-CAUSING DELTA-F508 MUTATION

Summary for 1CKW

• Entry DOI: 10.2210/pdb1ckw/pdb
• NMR Information: BMRB: 4595
• Descriptor: PROTEIN (CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR (CFTR)) (1 entity in total)
• Functional Keywords: p25_tfe, cystic fibrosis, peptides, metal transport
• Cellular location: Early endosome membrane; Multi-pass membrane protein (By similarity): Q00555
• Total number of polymer chains: 1
• Total formula weight: 2907.35

Authors

Massiah, M.A.,Ko, Y.H.,Pedersen, P.L.,Mildvan, A.S. (deposition date: 1999-04-26, release date: 1999-05-04, Last modification date: 2023-12-27)

Primary citation

Massiah, M.A.,Ko, Y.H.,Pedersen, P.L.,Mildvan, A.S.
Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation.
Biochemistry, 38:7453-7461, 1999

PubMed Abstract: Most cases of cystic fibrosis (CF), a common inherited disease of epithelial cell origin, are caused by the deletion of Phe508 located in the first nucleotide-binding domain (NBF1) of the protein called CFTR (cystic fibrosis transmembrane conductance regulator). To gain greater insight into the structure within the Phe508 region of the wild-type protein and the change in structure that occurs when this residue is deleted, we conducted nuclear magnetic resonance (NMR) studies on representative synthetic 26 and 25 amino acid peptide segments. 2D 1H NMR studies at 600 MHz of the 26-residue peptide consisting of Met498 to Ala523 in 10% DMSO, pH 4.0, at 25 degrees C show a continuous but labile helix from Gly500 to Lys522, based on both NH-NH(i,i+1) and alphaH-NH(i,i+1) NOEs. Phe508 within this helix shows only short-range (i, PubMed: 10360942
DOI: 10.1021/bi9903603

Experimental method

SOLUTION NMR