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von Willebrand factor conformation and adhesive function is modulated by an internalized water molecule.

Celikel R, Ruggeri ZM, Varughese KI
Nat Struct Biol 7 881-4 (2000)
Cited: 59 times
EuropePMC logo PMID: 11017197

Abstract

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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Related citations provided by authors (1)

  1. Crystal Structure of the Von Willebrand Factor A1 D Domain in Complex with the Function Blocking Nmc-4 DOMAIN IN COMPLEX WITH THE FUNCTION BLOCKING NMC-4 FAB. Celikel R, Varughese KI, Madhusudan, Yoshioka A, Ware J, Ruggeri ZM Nat. Struct. Biol. 5 189- (1998)

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