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3o8y
From Proteopedia
(Difference between revisions)
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| - | + | ==Stable-5-Lipoxygenase== | |
| - | === | + | <StructureSection load='3o8y' size='340' side='right' caption='[[3o8y]], [[Resolution|resolution]] 2.39Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3o8y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O8Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O8Y FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ALOX5, LOG5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arachidonate_5-lipoxygenase Arachidonate 5-lipoxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.34 1.13.11.34] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3o8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o8y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o8y RCSB], [http://www.ebi.ac.uk/pdbsum/3o8y PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://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. | ||
| - | + | 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> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Arachidonate 5-lipoxygenase]] | [[Category: Arachidonate 5-lipoxygenase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Bartlett, S G | + | [[Category: Bartlett, S G]] |
| - | [[Category: Boeglin, W E | + | [[Category: Boeglin, W E]] |
| - | [[Category: Brash, A R | + | [[Category: Brash, A R]] |
| - | [[Category: Gilbert, N C | + | [[Category: Gilbert, N C]] |
| - | [[Category: Neau, D B | + | [[Category: Neau, D B]] |
| - | [[Category: Newcomer, M E | + | [[Category: Newcomer, M E]] |
| - | [[Category: Waight, M T | + | [[Category: Waight, M T]] |
[[Category: Coactosin like protein]] | [[Category: Coactosin like protein]] | ||
[[Category: Cytosol]] | [[Category: Cytosol]] | ||
Revision as of 18:09, 25 December 2014
Stable-5-Lipoxygenase
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