Title : Two Cys residues essential for von Willebrand factor multimer assembly in the Golgi.

Pub. Date : 2007 Oct 2

PMID : 17895385






5 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Von Willebrand factor (VWF) dimerizes through C-terminal CK domains, and VWF dimers assemble into multimers in the Golgi by forming intersubunit disulfide bonds between D3 domains. Disulfides von Willebrand factor Homo sapiens
2 Von Willebrand factor (VWF) dimerizes through C-terminal CK domains, and VWF dimers assemble into multimers in the Golgi by forming intersubunit disulfide bonds between D3 domains. Disulfides von Willebrand factor Homo sapiens
3 Von Willebrand factor (VWF) dimerizes through C-terminal CK domains, and VWF dimers assemble into multimers in the Golgi by forming intersubunit disulfide bonds between D3 domains. Disulfides von Willebrand factor Homo sapiens
4 This arrangement of intersubunit disulfide bonds implies that the dimeric N-terminal D"D3 domains of VWF subunits align in a parallel orientation within VWF multimers. Disulfides von Willebrand factor Homo sapiens
5 This arrangement of intersubunit disulfide bonds implies that the dimeric N-terminal D"D3 domains of VWF subunits align in a parallel orientation within VWF multimers. Disulfides von Willebrand factor Homo sapiens