1M0Z

Crystal Structure of the von Willebrand Factor Binding Domain of Glycoprotein Ib alpha

1M0Z の概要

• エントリーDOI: 10.2210/pdb1m0z/pdb
• 関連するPDBエントリー: 1M10
• 分子名称: Glycoprotein Ib alpha (2 entities in total)
• 機能のキーワード: leucine-rich repeat, hemostasis, blood clotting
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P07359
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 64733.82

構造登録者

Huizinga, E.G.,Tsuji, S.,Romijn, R.A.P.,Schiphorst, M.E.,de Groot, P.G.,Sixma, J.J.,Gros, P. (登録日: 2002-06-16, 公開日: 2002-08-28, 最終更新日: 2021-11-10)

主引用文献

Huizinga, E.G.,Tsuji, S.,Romijn, R.A.,Schiphorst, M.E.,de Groot, P.G.,Sixma, J.J.,Gros, P.
Structures of glycoprotein Ibalpha and its complex with von Willebrand factor A1 domain.
Science, 297:1176-1179, 2002

PubMed Abstract: Transient interactions of platelet-receptor glycoprotein Ibalpha (GpIbalpha) and the plasma protein von Willebrand factor (VWF) reduce platelet velocity at sites of vascular damage and play a role in haemostasis and thrombosis. Here we present structures of the GpIbalpha amino-terminal domain and its complex with the VWF domain A1. In the complex, GpIbalpha wraps around one side of A1, providing two contact areas bridged by an area of solvated charge interaction. The structures explain the effects of gain-of-function mutations related to bleeding disorders and provide a model for shear-induced activation. These detailed insights into the initial interactions in platelet adhesion are relevant to the development of antithrombotic drugs.

PubMed: 12183630
DOI: 10.1126/science.107355

実験手法

X-RAY DIFFRACTION (1.85 Å)