1m10

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[[Image:1m10.png|left|200px]]
 
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{{STRUCTURE_1m10| PDB=1m10 | SCENE= }}
{{STRUCTURE_1m10| PDB=1m10 | SCENE= }}
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===Crystal structure of the complex of Glycoprotein Ib alpha and the von Willebrand Factor A1 Domain===
===Crystal structure of the complex of Glycoprotein Ib alpha and the von Willebrand Factor A1 Domain===
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{{ABSTRACT_PUBMED_12183630}}
{{ABSTRACT_PUBMED_12183630}}

Revision as of 10:26, 11 March 2013

Template:STRUCTURE 1m10

Contents

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.

About this Structure

1m10 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • Huizinga EG, Tsuji S, Romijn RA, Schiphorst ME, de Groot PG, Sixma JJ, Gros P. Structures of glycoprotein Ibalpha and its complex with von Willebrand factor A1 domain. Science. 2002 Aug 16;297(5584):1176-9. PMID:12183630 doi:10.1126/science.107355

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