1fns

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[[Image:1fns.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_1fns| PDB=1fns | SCENE= }}
{{STRUCTURE_1fns| PDB=1fns | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE VON WILLEBRAND FACTOR (VWF) A1 DOMAIN I546V MUTANT IN COMPLEX WITH THE FUNCTION BLOCKING FAB NMC4'''
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===CRYSTAL STRUCTURE OF THE VON WILLEBRAND FACTOR (VWF) A1 DOMAIN I546V MUTANT IN COMPLEX WITH THE FUNCTION BLOCKING FAB NMC4===
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==Overview==
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Platelet participation in hemostasis and arterial thrombosis requires the binding of glycoprotein (GP) Ibalpha to von Willebrand factor (vWF). Hemodynamic forces enhance this interaction, an effect mimicked by the substitution I546V in the vWF A1 domain. A water molecule becomes internalized near the deleted Ile methyl group. The change in hydrophobicity of the local environment causes positional changes propagated over a distance of 27 A. As a consequence, a major reorientation of a peptide plane occurs in a surface loop involved in GP Ibalpha binding. This distinct vWF conformation shows increased platelet adhesion and provides a structural model for the initial regulation of thrombus formation.
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(as it appears on PubMed at http://www.pubmed.gov), where 11017197 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11017197}}
==About this Structure==
==About this Structure==
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[[Category: Blood coagulation type 2b von willebrand disease]]
[[Category: Blood coagulation type 2b von willebrand disease]]
[[Category: Von willebrand factor]]
[[Category: Von willebrand factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:32:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:38:36 2008''

Revision as of 00:38, 1 July 2008

Image:1fns.png

Template:STRUCTURE 1fns

CRYSTAL STRUCTURE OF THE VON WILLEBRAND FACTOR (VWF) A1 DOMAIN I546V MUTANT IN COMPLEX WITH THE FUNCTION BLOCKING FAB NMC4

Template:ABSTRACT PUBMED 11017197

About this Structure

1FNS is a Single protein structure of sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.

Reference

von Willebrand factor conformation and adhesive function is modulated by an internalized water molecule., Celikel R, Ruggeri ZM, Varughese KI, Nat Struct Biol. 2000 Oct;7(10):881-4. PMID:11017197

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