1dth
From Proteopedia
METALLOPROTEASE
Structural highlights
FunctionVM1AD_CROAT Snake venom zinc metalloproteinase that causes hemorrhage by provoking the degradation of the sub-endothelial matrix proteins (fibronectin, laminin, type IV collagen, nidogen, and gelatins).[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMatrix metalloproteinase enzymes have been implicated in degenerative processes like tumor cell invasion, metastasis, and arthritis. Specific metalloproteinase inhibitors have been used to block tumor cell proliferation. We have examined the interaction of batimastat (BB-94) with a metalloproteinase [atrolysin C (Ht-d), EC 3.4.24.42] active site at 2.0-angstroms resolution (R = 16.8%). The title structure exhibits an unexpected binding geometry, with the thiophene ring deeply inserted into the primary specificity site. This unprecedented binding geometry dramatizes the significance of the cavernous primary specificity site, pointing the way for the design of a new generation of potential antitumor drugs. Batimastat, a potent matrix mealloproteinase inhibitor, exhibits an unexpected mode of binding.,Botos I, Scapozza L, Zhang D, Liotta LA, Meyer EF Proc Natl Acad Sci U S A. 1996 Apr 2;93(7):2749-54. PMID:8610113[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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