1dth | pdb_00001dth

METALLOPROTEASE

spinqualitylabelsall models 1dth, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1dth is a 2 chain structure with sequence from Crotalus atrox. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BAT, CA, ZN Activity: Atrolysin C, with EC number 3.4.24.42 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [VM1AD_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). 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 PubMed Matrix 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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