1hs6
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(New page: 200px<br /> <applet load="1hs6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hs6, resolution 1.95Å" /> '''STRUCTURE OF LEUKOT...)
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Revision as of 15:15, 12 November 2007
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STRUCTURE OF LEUKOTRIENE A4 HYDROLASE COMPLEXED WITH BESTATIN.
Overview
Leukotriene (LT) A(4) hydrolase/aminopeptidase (LTA4H) is a bifunctional, zinc enzyme that catalyzes the biosynthesis of LTB4, a potent lipid, chemoattractant involved in inflammation, immune responses, host defense, against infection, and PAF-induced shock. The high resolution crystal, structure of LTA4H in complex with the competitive inhibitor bestatin, reveals a protein folded into three domains that together create a deep, cleft harboring the catalytic Zn(2+) site. A bent and narrow pocket, shaped to accommodate the substrate LTA(4), constitutes a highly confined, binding region that can be targeted in the design of specific, anti-inflammatory agents. Moreover, the structure of the catalytic domain, is very similar to that of thermolysin and provides detailed insight into, mechanisms of catalysis, in particular the chemical strategy for the, unique epoxide hydrolase reaction that generates LTB(4).
About this Structure
1HS6 is a Single protein structure of sequence from Homo sapiens with ZN, YB, ACT, BES and IMD as ligands. Active as Leukotriene-A(4) hydrolase, with EC number 3.3.2.6 Full crystallographic information is available from OCA.
Reference
Crystal structure of human leukotriene A(4) hydrolase, a bifunctional enzyme in inflammation., Thunnissen MM, Nordlund P, Haeggstrom JZ, Nat Struct Biol. 2001 Feb;8(2):131-5. PMID:11175901
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