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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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| Main Authors: | , , , , , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
American Society for Biochemistry and Molecular Biology
2010
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| Assuntos: | |
| Acesso em linha: | 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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