Conformational activation of ADAMTS13

Significance We show that a CUB–spacer domain interaction impedes exposure of the ADAMTS13 spacer functional exosite, preventing ADAMTS13 from interacting effectively with its complementary binding site in the VWF A2 domain. This CUB–spacer interaction is disrupted by interaction with the C-terminal...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2014-12, Vol.111 (52), p.18578-18583
Hauptverfasser:	South, Kieron, Luken, Brenda M., Crawley, James T. B., Phillips, Rebecca, Thomas, Mari, Collins, Richard F., Deforche, Louis, Vanhoorelbeke, Karen, Lane, David A.
Format:	Artikel
Sprache:	eng
Schlagworte:	ADAM Proteins - blood ADAM Proteins - chemistry ADAM Proteins - genetics ADAMTS13 Protein Amino Acid Sequence Amino Acid Substitution Antibodies Antibodies, Monoclonal, Murine-Derived - chemistry Autoantibodies autoimmunity Binding sites Biological Sciences Blood Blood plasma blood vessels Collagens Enzyme Activation Epitopes Humans Immune system Kinetics Microscopy Mutation, Missense pathogenesis patients Proteases Protein Structure, Tertiary Proteins Purpura, Thrombotic Thrombocytopenic - enzymology Purpura, Thrombotic Thrombocytopenic - genetics Sequence Deletion Thrombotic thrombocytopenic purpura Truncation von Willebrand Factor - chemistry von Willebrand Factor - genetics von Willebrand Factor - metabolism
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