Platelet glycoprotein

From Proteopedia

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Revision as of 12:11, 12 January 2022

Platelet-receptor glycoprotein Ib alpha (blue) involved in Willebrand disease bound to the von Willebrand Factor A1 Domain (green surface), (1m10)

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1 Crystal structure of the complex of Glycoprotein Ib alpha and the von Willebrand Factor A1 Domain
2 Disease
3 About this Structure
4 Platelet glycoprotein 4

Crystal structure of the complex of Glycoprotein Ib alpha and the von Willebrand Factor A1 Domain

Publication Abstract from PubMed

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.

Structures of glycoprotein Ibalpha and its complex with von Willebrand factor A1 domain., Huizinga EG, Tsuji S, Romijn RA, Schiphorst ME, de Groot PG, Sixma JJ, Gros P, Science. 2002 Aug 16;297(5584):1176-9. PMID:12183630

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Disease

Known disease associated with this structure: von Willebrand disease, autosomal dominant OMIM:[193400], von Willebrand disease, autosomal recessive OMIM:[193400], Bernard-Soulier syndrome, benign autosomal dominant OMIM:[606672], Bernard-Soulier syndrome, type A OMIM:[606672], von Willebrand disease, platelet-type OMIM:[606672], Nonarteritic anterior ischemic optic neuropathy, susceptibility to OMIM:[606672]

About this Structure

1m10 is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.