1gw6: Difference between revisions

Revision as of 06:12, 1 July 2008

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File:1gw6.png

Template:STRUCTURE 1gw6

STRUCTURE OF LEUKOTRIENE A4 HYDROLASE D375N MUTANTSTRUCTURE OF LEUKOTRIENE A4 HYDROLASE D375N MUTANT

Template:ABSTRACT PUBMED 11917124

About this StructureAbout this Structure

1GW6 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Leukotriene A4 hydrolase: selective abrogation of leukotriene B4 formation by mutation of aspartic acid 375., Rudberg PC, Tholander F, Thunnissen MM, Samuelsson B, Haeggstrom JZ, Proc Natl Acad Sci U S A. 2002 Apr 2;99(7):4215-20. Epub 2002 Mar 26. PMID:11917124

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-'''STRUCTURE OF LEUKOTRIENE A4 HYDROLASE D375N MUTANT'''
+===STRUCTURE OF LEUKOTRIENE A4 HYDROLASE D375N MUTANT===
-==Overview==
+<!--
-Leukotriene A4 (LTA4, 5S-trans-5,6-oxido-7,9-trans-11,14-cis-eicosatetraenoic acid) hydrolase (LTA4H)/aminopeptidase is a bifunctional zinc metalloenzyme that catalyzes the final and rate-limiting step in the biosynthesis of leukotriene B4 (LTB4, 5S,12R-dihydroxy-6,14-cis-8,10-trans-eicosatetraenoic acid), a classical chemoattractant and immune modulating lipid mediator. Two chemical features are key to the bioactivity of LTB4, namely, the chirality of the 12R-hydroxyl group and the cis-trans-trans geometry of the conjugated triene structure. From the crystal structure of LTA4H, a hydrophilic patch composed of Gln-134, Tyr-267, and Asp-375 was identified in a narrow and otherwise hydrophobic pocket, believed to bind LTA4. In addition, Asp-375 belongs to peptide K21, a previously characterized 21-residue active site-peptide to which LTA4 binds during suicide inactivation. In the present report we used site-directed mutagenesis and x-ray crystallography to show that Asp-375, but none of the other candidate residues, is specifically required for the epoxide hydrolase activity of LTA4H. Thus, mutation of Asp-375 leads to a selective loss of the enzyme's ability to generate LTB4 whereas the aminopeptidase activity is preserved. We propose that Asp-375, possibly assisted by Gln-134, acts as a critical determinant for the stereoselective introduction of the 12R-hydroxyl group and thus the biological activity of LTB4.
+The line below this paragraph, {{ABSTRACT_PUBMED_11917124}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_11917124}}
 ==About this Structure==
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 [[Category: Hydrolase]]
 [[Category: Mutagenesis study]]
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