Flexibility of the Thrombin-activatable Fibrinolysis Inhibitor Pro-domain Enables Productive Binding of Protein Substrates

We have previously reported that thrombin-activatable fibrinolysis inhibitor (TAFI) exhibits intrinsic proteolytic activity toward large peptides. The structural basis for this observation was clarified by the crystal structures of human and bovine TAFI. These structures evinced a significant rotati...

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Autors principals: Valnickova, Zuzana, Sanglas, Laura, Arolas, Joan L., Petersen, Steen V., Schar, Christine, Otzen, Daniel, Aviles, Francesc X., Gomis-Rüth, F. Xavier, Enghild, Jan J.
Format: Artigo
Idioma:Inglês
Publicat: American Society for Biochemistry and Molecular Biology 2010
Matèries:
Protein Structure and Folding
Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC2992258/
https://ncbi.nlm.nih.gov/pubmed/20880845
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M110.150342
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