Title : von Willebrand factor is dimerized by protein disulfide isomerase.

Pub. Date : 2016 Mar 3

PMID : 26670633






3 Functional Relationships(s)
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1 VWF is dimerized in the endoplasmic reticulum by formation of disulfide bonds between the C-terminal cysteine knot (CK) domains of 2 monomers. Disulfides von Willebrand factor Homo sapiens
2 On the basis of protein-protein docking and molecular dynamics simulations, combined with fluorescence microscopy studies of VWF CK-domain mutants, we suggest the following mechanism of VWF dimerization: PDI initiates VWF dimerization by forming the first 2 disulfide bonds Cys2771-2773" and Cys2771"-2773. Disulfides von Willebrand factor Homo sapiens
3 On the basis of protein-protein docking and molecular dynamics simulations, combined with fluorescence microscopy studies of VWF CK-domain mutants, we suggest the following mechanism of VWF dimerization: PDI initiates VWF dimerization by forming the first 2 disulfide bonds Cys2771-2773" and Cys2771"-2773. Disulfides von Willebrand factor Homo sapiens