The structure of human 5-lipoxygenase.

Gilbert NC, Bartlett SG, Waight MT, Neau DB, Boeglin WE, Brash AR, Newcomer ME
Science. 2011 331 (6014): 217-9

PMID: 21233389 · PMCID: PMC3245680 · DOI:10.1126/science.1197203

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.

MeSH Terms (13)

Amino Acid Sequence Arachidonate 5-Lipoxygenase Catalytic Domain Crystallography, X-Ray Enzyme Stability Humans Iron Models, Molecular Molecular Sequence Data Mutant Proteins Protein Folding Protein Structure, Secondary Protein Structure, Tertiary

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