Ontology highlight
ABSTRACT:
SUBMITTER: Petri A
PROVIDER: S-EPMC6706451 | biostudies-literature | 2019 Aug
REPOSITORIES: biostudies-literature
Petri Anastasis A Kim Hyo Jung HJ Xu Yaoxian Y de Groot Rens R Li Chan C Vandenbulcke Aline A Vanhoorelbeke Karen K Emsley Jonas J Crawley James T B JTB
Nature communications 20190822 1
Platelet recruitment to sites of blood vessel damage is highly dependent upon von Willebrand factor (VWF). VWF platelet-tethering function is proteolytically regulated by the metalloprotease ADAMTS13. Proteolysis depends upon shear-induced conformational changes in VWF that reveal the A2 domain cleavage site. Multiple ADAMTS13 exosite interactions are involved in recognition of the unfolded A2 domain. Here we report through kinetic analyses that, in binding VWF, the ADAMTS13 cysteine-rich and sp ...[more]