1gw6
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STRUCTURE OF LEUKOTRIENE A4 HYDROLASE D375N MUTANT
OverviewOverview
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 ... [(full description)]
About this StructureAbout this Structure
1GW6 is a [Single protein] structure of sequence from [Homo sapiens] with ACT, YB, ZN, BES and IMD as [ligands]. Active as [[1]], with EC number [3.3.2.6]. 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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