1bmm
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(New page: 200px<br /> <applet load="1bmm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bmm, resolution 2.6Å" /> '''HUMAN ALPHA-THROMBIN...)
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Revision as of 16:43, 29 October 2007
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HUMAN ALPHA-THROMBIN COMPLEXED WITH [S-(R*,R*)]-4-[(AMINOIMINOMETHYL)AMINO]-N-[[1-[3-HYDROXY-2-[(2-NAPHTHALENYLSULFONYL)AMINO]-1-OXOPROPYL]-2-PYRROLIDINYL] METHYL]BUTANAMIDE (BMS-186282)
Overview
The crystallographic structures of the ternary complexes of human, alpha-thrombin with hirugen (a sulfated hirudin fragment) and the, small-molecule active site thrombin inhibitors BMS-186282 and BMS-189090, have been determined at 2.6 and 2.8 A. In both cases, the inhibitors, which adopt very similar bound conformations, bind in an antiparallel, beta-strand arrangement relative to the thrombin main chain in a manner, like that reported for PPACK, D-Phe-Pro-Arg-CH2Cl. They do, however, exhibit differences in the binding of the alkyl guanidine moiety in the, specificity pocket. Numerous hydrophilic and hydrophobic interactions, serve to stabilize the inhibitors in the binding pocket. Although PPACK, forms covalent bonds to both serine and the histidine of the catalytic, triad of thrombin, ... [(full description)]
About this Structure
1BMM is a [Protein complex] structure of sequences from [Hirudo medicinalis] and [Homo sapiens] with BM2 as [ligand]. Active as [[1]], with EC number [3.4.21.5]. Full crystallographic information is available from [OCA].
Reference
Crystallographic determination of the structures of human alpha-thrombin complexed with BMS-186282 and BMS-189090., Malley MF, Tabernero L, Chang CY, Ohringer SL, Roberts DG, Das J, Sack JS, Protein Sci. 1996 Feb;5(2):221-8. PMID:8745399
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