1AO3

A3 DOMAIN OF VON WILLEBRAND FACTOR

1AO3 の概要

• エントリーDOI: 10.2210/pdb1ao3/pdb
• 分子名称: VON WILLEBRAND FACTOR (2 entities in total)
• 機能のキーワード: collagen-binding, von willebrand, cell adhesion
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39899.62

構造登録者

Bienkowski, J.,Cruz, M.,Handin, R.,Liddington, R. (登録日: 1997-07-16, 公開日: 1998-07-22, 最終更新日: 2024-10-09)

主引用文献

Bienkowska, J.,Cruz, M.,Atiemo, A.,Handin, R.,Liddington, R.
The von willebrand factor A3 domain does not contain a metal ion-dependent adhesion site motif.
J.Biol.Chem., 272:25162-25167, 1997

PubMed Abstract: von Willebrand factor (vWF) is a multimeric plasma protein that mediates platelet adhesion to exposed subendothelium at sites of vascular injury. The A3 domain of vWF (vWF-A3) forms the principal binding site for collagens type I and III. We report here the crystal structure of the vWF-A3 domain at 2.2-A resolution. As expected, the structure is similar to the integrin I domain but with several novel features. Sequence alignments had suggested that the domain contained an integrin metal ion-dependent adhesion site (MIDAS) motif, but the crystal structure shows that the motif is modified and that no metal ion is bound. We have introduced mutations into the vestigial MIDAS motif and report that, unlike the I domain of integrin alpha2beta1, vWF-A3 continues to bind collagen after disruption of the motif. We conclude that collagen recognition by vWF-A3 occurs by a mechanism different from that of the integrin alpha2beta1.

PubMed: 9312128
DOI: 10.1074/jbc.272.40.25162

実験手法

X-RAY DIFFRACTION (2.2 Å)