4IHK

Crystal structure of the Collagen VI alpha3 N5 domain R1061Q

4IHK の概要

• エントリーDOI: 10.2210/pdb4ihk/pdb
• 関連するPDBエントリー: 4IGI
• 分子名称: Collagen alpha3(VI) (2 entities in total)
• 機能のキーワード: cell adhesion, collagen vi 3n5, vwa
• 由来する生物種: Mus musculus (mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21682.65

構造登録者

Mikolajek, H.,Becker, A.K.A.,Paulsson, M.,Wagener, R.,Werner, J.M. (登録日: 2012-12-19, 公開日: 2013-12-18, 最終更新日: 2023-11-08)

主引用文献

Becker, A.K.,Mikolajek, H.,Paulsson, M.,Wagener, R.,Werner, J.M.
A structure of a collagen VI VWA domain displays N and C termini at opposite sides of the protein
Structure, 22:199-208, 2014

PubMed Abstract: Von Willebrand factor A (VWA) domains are versatile protein interaction domains with N and C termini in close proximity placing spatial constraints on overall protein structure. The 1.2 Å crystal structures of a collagen VI VWA domain and a disease-causing point mutant show C-terminal extensions that place the N and C termini at opposite ends. This allows a "beads-on-a-string" arrangement of multiple VWA domains as observed for ten N-terminal domains of the collagen VI α3 chain. The extension is linked to the core domain by a salt bridge and two hydrophobic patches. Comparison of the wild-type and a muscular dystrophy-associated mutant structure identifies a potential perturbation of a protein interaction interface and indeed, the secretion of mutant collagen VI tetramers is affected. Homology modeling is used to locate a number of disease-associated mutations and analyze their structural impact, which will allow mechanistic analysis of collagen-VI-associated muscular dystrophy phenotypes.

PubMed: 24332716
DOI: 10.1016/j.str.2013.06.028

実験手法

X-RAY DIFFRACTION (1.2 Å)