Structural highlights
Function
LOX5_HUMAN Catalyzes the first step in leukotriene biosynthesis, and thereby plays a role in inflammatory processes.[1]
Publication Abstract from PubMed
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.
The structure of human 5-lipoxygenase.,Gilbert NC, Bartlett SG, Waight MT, Neau DB, Boeglin WE, Brash AR, Newcomer ME Science. 2011 Jan 14;331(6014):217-9. PMID:21233389[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. PMID:21233389 doi:10.1126/science.1197203
- ↑ 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. PMID:21233389 doi:10.1126/science.1197203
