The structure of human 5-lipoxygenase.

Article Details

Citation

Gilbert NC, Bartlett SG, Waight MT, Neau DB, Boeglin WE, Brash AR, Newcomer ME

The structure of human 5-lipoxygenase.

Science. 2011 Jan 14;331(6014):217-9. doi: 10.1126/science.1197203.

PubMed ID
21233389 [ View in PubMed
]
Abstract

The synthesis of both proinflammatory leukotrienes and anti-inflammatory lipoxins requires the enzyme 5-lipoxygenase (5-LOX). 5-LOX activity is short-lived, apparently in part because of an intrinsic instability of the enzyme. We identified a 5-LOX-specific destabilizing sequence that is involved in orienting the carboxyl terminus, which binds the catalytic iron. Here, we report the crystal structure at 2.4 angstrom resolution of human 5-LOX stabilized by replacement of this sequence.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Arachidonate 5-lipoxygenaseP09917Details