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1bmm

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[[Image:1bmm.gif|left|200px]]
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{{STRUCTURE_1bmm| PDB=1bmm | SCENE= }}
{{STRUCTURE_1bmm| PDB=1bmm | SCENE= }}
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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)'''
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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)===
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==Overview==
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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, neither BMS-186282 nor BMS-189090 bind covalently and only BMS-186282 forms a hydrogen bond to the serine of the catalytic triad. Both inhibitors bind with high affinity (Ki = 79 nM and 3.6 nM, respectively) and are highly selective for thrombin over trypsin and other serine proteases.
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(as it appears on PubMed at http://www.pubmed.gov), where 8745399 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8745399}}
==About this Structure==
==About this Structure==
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[[Category: Sack, J.]]
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[[Category: Hydrolase]]
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Revision as of 16:23, 30 June 2008

Image:1bmm.png

Template:STRUCTURE 1bmm

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)

Template:ABSTRACT PUBMED 8745399

About this Structure

1BMM is a Protein complex structure of sequences from Hirudo medicinalis and Homo sapiens. 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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