3o8y
From Proteopedia
(Difference between revisions)
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/LOX5_HUMAN LOX5_HUMAN] Catalyzes the first step in leukotriene biosynthesis, and thereby plays a role in inflammatory processes.<ref>PMID:21233389</ref> | [https://www.uniprot.org/uniprot/LOX5_HUMAN LOX5_HUMAN] Catalyzes the first step in leukotriene biosynthesis, and thereby plays a role in inflammatory processes.<ref>PMID:21233389</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == 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. | ||
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| - | 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<ref>PMID:21233389</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3o8y" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Stable-5-Lipoxygenase
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Categories: Homo sapiens | Large Structures | Bartlett SG | Boeglin WE | Brash AR | Gilbert NC | Neau DB | Newcomer ME | Waight MT
