| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5371273 | Biophysical Chemistry | 2012 | 11 Pages |
Abstract
⺠The three-dimensional model of ADAMTS13 metalloprotease domain (M13) was built by homology modeling techniques. ⺠The model was validated against all known artificial and natural mutations found in M13 sequence. ⺠The peptide vWF(1604-1607) of von Willebrand factor (vWF) was docked into the protease active site. ⺠The docking model explains why oxidation of Met1606 to methionine sulfoxide inhibits vWF proteolysis by ADAMTS13. ⺠The model explains why Val1607Asp mutation in type 2A von Willebrand disease accelerates proteolysis of vWF by ADAMTS13.
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Physical Sciences and Engineering
Chemistry
Physical and Theoretical Chemistry
Authors
Nicola Pozzi, Stefano Lancellotti, Raimondo De Cristofaro, Vincenzo De Filippis,