1m0z
From Proteopedia
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==Disease== | ==Disease== | ||
- | Known disease associated with this structure: Bernard-Soulier syndrome, type A OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=606672 606672]], von Willebrand disease, platelet-type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=606672 606672]], Nonarteritic anterior ischemic optic neuropathy, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=606672 606672]] | + | Known disease associated with this structure: Bernard-Soulier syndrome, benign autosomal dominant OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=606672 606672]], Bernard-Soulier syndrome, type A OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=606672 606672]], von Willebrand disease, platelet-type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=606672 606672]], Nonarteritic anterior ischemic optic neuropathy, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=606672 606672]] |
==About this Structure== | ==About this Structure== | ||
- | 1M0Z is a | + | 1M0Z is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M0Z OCA]. |
==Reference== | ==Reference== | ||
- | + | <ref group="xtra">PMID:12183630</ref><references group="xtra"/> | |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: Single protein]] | ||
[[Category: Groot, P G.de.]] | [[Category: Groot, P G.de.]] | ||
[[Category: Gros, P.]] | [[Category: Gros, P.]] | ||
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[[Category: Leucine-rich repeat]] | [[Category: Leucine-rich repeat]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 09:06:59 2009'' |
Revision as of 07:07, 17 February 2009
Contents |
Crystal Structure of the von Willebrand Factor Binding Domain of Glycoprotein Ib alpha
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: 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
1M0Z is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
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
Page seeded by OCA on Tue Feb 17 09:06:59 2009