1m0z: Difference between revisions

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

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

~~==Overview==~~

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~~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.

The line below this paragraph, {{ABSTRACT_PUBMED_12183630}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12183630 is the PubMed ID number.

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==Disease==

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[[Category: Hemostasis]]

[[Category: Leucine-rich repeat]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May~~ ~~3 00~~:29:58 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 22:58:41 2008''

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-[[Image:1m0z.jpg|left|200px]]
+{{Seed}}
+[[Image:1m0z.png|left|200px]]
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 {{STRUCTURE_1m0z|  PDB=1m0z  |  SCENE=  }}
-'''Crystal Structure of the von Willebrand Factor Binding Domain of Glycoprotein Ib alpha'''
+===Crystal Structure of the von Willebrand Factor Binding Domain of Glycoprotein Ib alpha===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12183630}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12183630 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12183630}}
 ==Disease==
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 [[Category: Hemostasis]]
 [[Category: Leucine-rich repeat]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:29:58 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 22:58:41 2008''