Crystal structure and substrate-induced activation of adamts13

HIGHLIGHTS

• who: Anastasis Petri from the College University of have published the research: Crystal structure and substrate-induced activation of ADAMTS13, in the Journal: NATURE COMMUNICATIONS NATURE COMMUNICATIONS
• what: Using kinetic analysis of substrate proteolysis, the authors demonstrate that, in binding VWF, the ADAMTS13 Cys-rich and Spacer domain exosites bring the enzyme and the unfolded VWF A2 domain into proximity. Given the data revealing the functional importance of the hydrophobic VWF residues Leu1664, Val1665, and Leu1666 in binding the Spacer domain exosite, | https://doi.org/10.1038/s41467-019-11474-5 MP Dis Cys TSP1 . . .
  

   

  

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