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| [[Image:1lhg.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1lhg| PDB=1lhg | SCENE= }} | | {{STRUCTURE_1lhg| PDB=1lhg | SCENE= }} |
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| '''HUMAN ALPHA-THROMBIN COMPLEXED WITH AC-(D)PHE-PRO-BOROORNITHINE-OH'''
| | ===HUMAN ALPHA-THROMBIN COMPLEXED WITH AC-(D)PHE-PRO-BOROORNITHINE-OH=== |
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| ==Overview==
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| The X-ray crystallographic structure of Ac-(D)Phe-Pro-boroArg-OH [DuP714, Ki = 0.04 nM; Kettner, C., Mersinger, L., & Knabb, R. (1990) J. Biol. Chem. 265, 18289] complexed with human alpha-thrombin shows the boron atom covalently bonded to the side-chain oxygen of the active site serine, Ser195. The boron adopts a nearly tetrahedral geometry, and the boronic acid forms a set of interactions with the protein that mimic the tetrahedral transition state of serine proteases. Contributions of the arginine side chain to inhibitor affinity were examined by synthesis of the ornithine, lysine, homolysine, and amidine analogs of DuP714. The basic groups interact with backbone carbonyl groups, water molecules, and an aspartic acid side chain (Asp189) located in the thrombin S1 specificity pocket. The variation in inhibition constant by 3 orders of magnitude appears to reflect differences in the energetics of interactions made with thrombin and differences in ligand flexibility in solution.(ABSTRACT TRUNCATED AT 250 WORDS) | | The line below this paragraph, {{ABSTRACT_PUBMED_7893672}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 7893672 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_7893672}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Vitamin k]] | | [[Category: Vitamin k]] |
| [[Category: Zymogen]] | | [[Category: Zymogen]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:55:18 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 20:54:40 2008'' |