| Literature DB >> 7712286 |
M T Stubbs1, W Bode.
Abstract
A comprehensive three-dimensional picture of the coagulation process is beginning to emerge. Crystallographic structure determinations of prothrombin, factor Xa, factor IXa, tissue factor and factor XIII represent important advances in our understanding of the coagulation cascade. Similarly, structures of antithrombin, tissue factor pathway inhibitor and thrombomodulin provide details of endogenous anticoagulatory mechanisms. NMR spectroscopy of multiple domains of coagulation proteins represents an important contribution to the analysis of flexibility and rigidity of modular proteins. Thrombin, as the prime candidate for antithrombotic drug design, continues to be an object of intense efforts in applied crystallography.Entities:
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Year: 1994 PMID: 7712286 DOI: 10.1016/0959-440x(94)90263-1
Source DB: PubMed Journal: Curr Opin Struct Biol ISSN: 0959-440X Impact factor: 6.809