3VI4

Crystal structure of alpha5beta1 integrin headpiece in complex with RGD peptide

3VI4 の概要

• エントリーDOI: 10.2210/pdb3vi4/pdb
• 分子名称: Integrin alpha-5, MAGNESIUM ION, Integrin beta-1, ... (10 entities in total)
• 機能のキーワード: beta propeller fold, rossmann fold, beta sandwich, fibronectin receptor, cell adhesion-immune system complex, cell adhesion/immune system
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 339884.39

構造登録者

Nagae, M.,Nogi, T.,Takagi, J. (登録日: 2011-09-21, 公開日: 2012-02-22, 最終更新日: 2024-11-20)

主引用文献

Nagae, M.,Re, S.,Mihara, E.,Nogi, T.,Sugita, Y.,Takagi, J.
Crystal structure of alpha5beta1 integrin ectodomain: Atomic details of the fibronectin receptor
J.Cell Biol., 197:131-140, 2012

PubMed Abstract: Integrin α5β1 is a major cellular receptor for the extracellular matrix protein fibronectin and plays a fundamental role during mammalian development. A crystal structure of the α5β1 integrin headpiece fragment bound by an allosteric inhibitory antibody was determined at a 2.9-Å resolution both in the absence and presence of a ligand peptide containing the Arg-Gly-Asp (RGD) sequence. The antibody-bound β1 chain accommodated the RGD ligand with very limited structural changes, which may represent the initial step of cell adhesion mediated by nonactivated integrins. Furthermore, a molecular dynamics simulation pointed to an important role for Ca(2+) in the conformational coupling between the ligand-binding site and the rest of the molecule. The RGD-binding pocket is situated at the center of a trenchlike exposed surface on the top face of α5β1 devoid of glycosylation sites. The structure also enabled the precise prediction of the acceptor residue for the auxiliary synergy site of fibronectin on the α5 subunit, which was experimentally confirmed by mutagenesis and kinetic binding assays.

PubMed: 22451694
DOI: 10.1083/jcb.201111077

実験手法

X-RAY DIFFRACTION (2.9 Å)