Leukotriene A4 Hydrolase

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== Disease ==
== Disease ==
Mutations in LTA4H are linked to susceptibility to asthma and to cardiovascular disease.
Mutations in LTA4H are linked to susceptibility to asthma and to cardiovascular disease.
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== Structural highlights ==
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LTA4H structure shows 3 domains: N-terminal, catalytic and C-terminal. The catalytic domain is made of 2 lobes: an α-helical one and an α/β one. The catalytic site is located between the 2 lobes and contains a Zn+2 ion<ref>PMID:11175901</ref> .
== 3D Structures of Leukotriene A4 Hydrolase ==
== 3D Structures of Leukotriene A4 Hydrolase ==

Revision as of 06:35, 13 April 2016

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

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Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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