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

1CKW の概要

• エントリーDOI: 10.2210/pdb1ckw/pdb
• NMR情報: BMRB: 4595
• 分子名称: PROTEIN (CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR (CFTR)) (1 entity in total)
• 機能のキーワード: p25_tfe, cystic fibrosis, peptides, metal transport
• 細胞内の位置: Early endosome membrane; Multi-pass membrane protein (By similarity): Q00555
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2907.35

構造登録者

Massiah, M.A.,Ko, Y.H.,Pedersen, P.L.,Mildvan, A.S. (登録日: 1999-04-26, 公開日: 1999-05-04, 最終更新日: 2023-12-27)

主引用文献

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

実験手法

SOLUTION NMR