2aig
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(New page: 200px<br /><applet load="2aig" size="450" color="white" frame="true" align="right" spinBox="true" caption="2aig, resolution 2.6Å" /> '''ADAMALYSIN II WITH PE...)
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Revision as of 06:01, 21 November 2007
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ADAMALYSIN II WITH PEPTIDOMIMETIC INHIBITOR POL647
Overview
Crotalus adamanteus snake venom adamalysin II is the structural prototype, of the adamalysin or ADAM family comprising proteolytic domains of snake, venom metalloproteinases, multimodular mammalian reproductive tract, proteins, and tumor necrosis factor alpha convertase, TACE, involved in, the release of the inflammatory cytokine, TNFalpha. The structure of, adamalysin II in noncovalent complex with two small-molecule right-hand, side peptidomimetic inhibitors (Pol 647 and Pol 656) has been solved using, X-ray diffraction data up to 2.6 and 2.8 A resolution. The inhibitors bind, to the S'-side of the proteinase, inserting between two protein segments, establishing a mixed parallel-antiparallel three-stranded beta-sheet and, coordinate the central zinc ion in a bidentate manner via their two, C-terminal oxygen atoms. The proteinase-inhibitor complexes are described, in detail and are compared with other known structures. An, adamalysin-based model of the active site of TACE reveals that these small, molecules would probably fit into the active site cleft of this latter, metalloproteinase, providing a starting model for the rational design of, TACE inhibitors.
About this Structure
2AIG is a Single protein structure of sequence from Crotalus adamanteus with ZN, CA and SO4 as ligands. Active as Adamalysin, with EC number 3.4.24.46 Full crystallographic information is available from OCA.
Reference
Structures of adamalysin II with peptidic inhibitors. Implications for the design of tumor necrosis factor alpha convertase inhibitors., Gomis-Ruth FX, Meyer EF, Kress LF, Politi V, Protein Sci. 1998 Feb;7(2):283-92. PMID:9521103
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