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.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
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.
|
| skos:exactMatch | |
| uniprot:name |
Science
|
| uniprot:author |
Bartlett S.G.,
Boeglin W.E.,
Brash A.R.,
Gilbert N.C.,
Neau D.B.,
Newcomer M.E.,
Waight M.T.
|
| uniprot:date |
2011
|
| uniprot:pages |
217-219
|
| uniprot:title |
The structure of human 5-lipoxygenase.
|
| uniprot:volume |
331
|
| dc-term:identifier |
doi:10.1126/science.1197203
|