Control of VWF A2 domain stability and ADAMTS13 access to the scissile bond of full-length VWF

Blood20.30
Volume: 123, Issue: 16, Pages: 2585 - 2592
Published: Apr 17, 2014
Abstract
Rheological shear forces in the blood trigger von Willebrand factor (VWF) unfolding which exposes the Y1605-M1606 scissile bond within the VWF A2 domain for cleavage by ADAMTS13. The VWF A2 domain contains 2 structural features that provide it with stability: a vicinal disulphide bond and a Ca(2+)-binding site (CBS). We investigated how these 2 structural features interplay to determine stability and regulate the exposure of the scissile bond in...
Paper Details
Title
Control of VWF A2 domain stability and ADAMTS13 access to the scissile bond of full-length VWF
Published Date
Apr 17, 2014
Journal
Volume
123
Issue
16
Pages
2585 - 2592
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