1XFA

Structure of NBD1 from murine CFTR- F508R mutant

1XFA の概要

• エントリーDOI: 10.2210/pdb1xfa/pdb
• 関連するPDBエントリー: 1XF9
• 分子名称: Cystic fibrosis transmembrane conductance regulator, MAGNESIUM ION, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: cystic fibrosis, abc transporters, atp, nucleotide-binding domain, transport protein
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Early endosome membrane; Multi-pass membrane protein (By similarity): P26361
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 64932.17

構造登録者

Thibodeau, P.H.,Brautigam, C.A.,Machius, M.,Thomas, P.J. (登録日: 2004-09-14, 公開日: 2004-12-28, 最終更新日: 2023-08-23)

主引用文献

Thibodeau, P.H.,Brautigam, C.A.,Machius, M.,Thomas, P.J.
Side chain and backbone contributions of Phe508 to CFTR folding.
Nat.Struct.Mol.Biol., 12:10-16, 2005

PubMed Abstract: Mutations in the cystic fibrosis transmembrane conductance regulator (CFTR), an integral membrane protein, cause cystic fibrosis (CF). The most common CF-causing mutant, deletion of Phe508, fails to properly fold. To elucidate the role Phe508 plays in the folding of CFTR, missense mutations at this position were generated. Only one missense mutation had a pronounced effect on the stability and folding of the isolated domain in vitro. In contrast, many substitutions, including those of charged and bulky residues, disrupted folding of full-length CFTR in cells. Structures of two mutant nucleotide-binding domains (NBDs) reveal only local alterations of the surface near position 508. These results suggest that the peptide backbone plays a role in the proper folding of the domain, whereas the side chain plays a role in defining a surface of NBD1 that potentially interacts with other domains during the maturation of intact CFTR.

PubMed: 15619636
DOI: 10.1038/nsmb881

実験手法

X-RAY DIFFRACTION (3.1 Å)