THE INTACT AND CLEAVED HUMAN ANTITHROMBIN-III COMPLEX AS A MODEL FOR SERPIN-PROTEINASE INTERACTIONS
作者： Herman A. Schreuder , Bijtske de Boer , Rein Dijkema , John Mulders , Henri J. M. Theunissen
DOI: 10.1038/NSB0194-48
关键词:
摘要: Antithrombin is a member of the serine proteinase inhibitor (serpin) family which contain flexible reactive site loop that interacts with, and cleaved by target proteinase. In latent serpins, inserted into large central beta-sheet in same molecule, whereas ovalbumin, nonfunctional serpin, completely exposed an alpha-heliacal conformation. however neither conformation can bind to proteinases. here we report structure intact human antithrombin complex. The novel seems well suited for interaction with proteinases such as thrombin blood coagulation factor Xa.
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