4BJ3

Integrin alpha2 I domain E318W-collagen complex

4BJ3 の概要

• エントリーDOI: 10.2210/pdb4bj3/pdb
• 分子名称: INTEGRIN ALPHA-2, GFOGER PEPTIDE, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: cell adhesion
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P17301
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 56613.46

構造登録者

Carafoli, F.,Hamaia, S.W.,Bihan, D.,Hohenester, E.,Farndale, R.W. (登録日: 2013-04-16, 公開日: 2013-11-20, 最終更新日: 2023-12-20)

主引用文献

Carafoli, F.,Hamaia, S.W.,Bihan, D.,Hohenester, E.,Farndale, R.W.
An Activating Mutation Reveals a Second Binding Mode of the Integrin Alpha2 I Domain to the Gfoger Motif in Collagens.
Plos One, 8:69833-, 2013

PubMed Abstract: The GFOGER motif in collagens (O denotes hydroxyproline) represents a high-affinity binding site for all collagen-binding integrins. Other GxOGER motifs require integrin activation for maximal binding. The E318W mutant of the integrin α2β1 I domain displays a relaxed collagen specificity, typical of an active state. E318W binds more strongly than the wild-type α2 I domain to GMOGER, and forms a 2:1 complex with a homotrimeric, collagen-like, GFOGER peptide. Crystal structure analysis of this complex reveals two E318W I domains, A and B, bound to a single triple helix. The E318W I domains are virtually identical to the collagen-bound wild-type I domain, suggesting that the E318W mutation activates the I domain by destabilising the unligated conformation. E318W I domain A interacts with two collagen chains similarly to wild-type I domain (high-affinity mode). E318W I domain B makes favourable interactions with only one collagen chain (low-affinity mode). This observation suggests that single GxOGER motifs in the heterotrimeric collagens V and IX may support binding of activated integrins.

PubMed: 23922814
DOI: 10.1371/JOURNAL.PONE.0069833

実験手法

X-RAY DIFFRACTION (3.042 Å)