The ADAMTS13 metalloprotease domain: roles of subsites in enzyme activity and specificity.

@article{Groot2010TheAM,
  title={The ADAMTS13 metalloprotease domain: roles of subsites in enzyme activity and specificity.},
  author={Rens de Groot and David A Lane and James T B Crawley},
  journal={Blood},
  year={2010},
  volume={116 16},
  pages={
          3064-72
        }
}
ADAMTS13 modulates von Willebrand factor (VWF) platelet-tethering function by proteolysis of the Tyr1605-Met1606 bond in the VWF A2 domain. To examine the role of the metalloprotease domain of ADAMTS13 in scissile bond specificity, we identified 3 variable regions (VR1, -2, and -3) in the ADAMTS family metalloprotease domain that flank the active site, which might be important for specificity. Eight composite sequence swaps (to residues in ADAMTS1 or ADAMTS2) and 18 single-point mutants were… CONTINUE READING

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Essential role of the disintegrin-like domain in ADAMTS13 function

R de Groot, A Bardhan, N Ramroop, DA Lane, JT. Crawley
  • Blood
  • 2009