Leukotriene A4 Hydrolase

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Revision as of 09:36, 7 July 2019

Human leukotriene A4 Hydrolase complex with bestatin, acetate, imidazole, Yb+3 (green) and Zn+2 (grey) ions (PDB entry 1hs6)

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Updated on 07-July-2019

↑ Paige M, Wang K, Burdick M, Park S, Cha J, Jeffery E, Sherman N, Shim YM. Role of leukotriene A4 hydrolase aminopeptidase in the pathogenesis of emphysema. J Immunol. 2014 Jun 1;192(11):5059-68. doi: 10.4049/jimmunol.1400452. Epub 2014, Apr 25. PMID:24771855 doi:http://dx.doi.org/10.4049/jimmunol.1400452
↑ Fourie AM. Modulation of inflammatory disease by inhibitors of leukotriene A4 hydrolase. Curr Opin Investig Drugs. 2009 Nov;10(11):1173-82. PMID:19876785
↑ Thunnissen MM, Nordlund P, Haeggstrom JZ. Crystal structure of human leukotriene A(4) hydrolase, a bifunctional enzyme in inflammation. Nat Struct Biol. 2001 Feb;8(2):131-5. PMID:11175901 doi:10.1038/84117

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 == Structural highlights ==
-LTA4H structure shows <scene name='43/433034/Cv/2'>3 domains: N-terminal, catalytic and C-terminal</scene>.  The catalytic domain is made of 2 lobes: an α-helical one and an α/β one.  The <scene name='43/433034/Cv/5'>catalytic site</scene> is located between the 2 lobes and <scene name='43/433034/Cv/6'>contains a Zn+2 ion</scene><ref>PMID:11175901</ref>. Water molecules shown as red spheres.
+LTA4H structure shows <scene name='43/433034/Cv/10'>3 domains: N-terminal, catalytic and C-terminal</scene>.  The catalytic domain is made of 2 lobes: an α-helical one and an α/β one. The <scene name='43/433034/Cv/11'>catalytic site</scene> is located between the 2 lobes and <scene name='43/433034/Cv/12'>contains a Zn+2 ion</scene><ref>PMID:11175901</ref>. Water molecules shown as red spheres.
 <scene name='43/433034/Cv/8'>1st Yb coordination site</scene>.