1lhd
From Proteopedia
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'''HUMAN ALPHA-THROMBIN COMPLEXED WITH AC-(D)PHE-PRO-BOROLYS-OH''' | '''HUMAN ALPHA-THROMBIN COMPLEXED WITH AC-(D)PHE-PRO-BOROLYS-OH''' | ||
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[[Category: Schadt, M C.]] | [[Category: Schadt, M C.]] | ||
[[Category: Weber, P C.]] | [[Category: Weber, P C.]] | ||
| - | [[Category: | + | [[Category: Acute phase]] |
| - | [[Category: | + | [[Category: Blood coagulation]] |
| - | [[Category: | + | [[Category: Calcium-binding]] |
| - | [[Category: | + | [[Category: Disease mutation]] |
| - | + | [[Category: Duplication]] | |
| - | [[Category: | + | [[Category: Gamma-carboxyglutamic acid]] |
| - | [[Category: | + | [[Category: Glycoprotein]] |
| - | [[Category: | + | [[Category: Hydrolase]] |
| - | [[Category: | + | [[Category: Kringle]] |
| - | [[Category: | + | [[Category: Liver]] |
| - | [[Category: | + | [[Category: Plasma]] |
| - | [[Category: | + | [[Category: Serine protease]] |
| - | [[Category: | + | [[Category: Signal]] |
| - | [[Category: | + | [[Category: Vitamin k]] |
| - | [[Category: | + | [[Category: Zymogen]] |
| - | [[Category: | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:54:58 2008'' |
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Revision as of 20:55, 2 May 2008
HUMAN ALPHA-THROMBIN COMPLEXED WITH AC-(D)PHE-PRO-BOROLYS-OH
Overview
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)
About this Structure
1LHD is a Protein complex structure of sequences from Hirudo medicinalis and Homo sapiens. Full crystallographic information is available from OCA.
Reference
Kinetic and crystallographic studies of thrombin with Ac-(D)Phe-Pro-boroArg-OH and its lysine, amidine, homolysine, and ornithine analogs., Weber PC, Lee SL, Lewandowski FA, Schadt MC, Chang CW, Kettner CA, Biochemistry. 1995 Mar 21;34(11):3750-7. PMID:7893672 Page seeded by OCA on Fri May 2 23:54:58 2008
Categories: Hirudo medicinalis | Homo sapiens | Protein complex | Thrombin | Chang, C H. | Kettner, C A. | Lee, S L. | Lewandowski, F A. | Schadt, M C. | Weber, P C. | Acute phase | Blood coagulation | Calcium-binding | Disease mutation | Duplication | Gamma-carboxyglutamic acid | Glycoprotein | Hydrolase | Kringle | Liver | Plasma | Serine protease | Signal | Vitamin k | Zymogen
