4nre

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:34, 1 March 2024) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
 +
==The structure of human 15-lipoxygenase-2 with a substrate mimic==
==The structure of human 15-lipoxygenase-2 with a substrate mimic==
-
<StructureSection load='4nre' size='340' side='right' caption='[[4nre]], [[Resolution|resolution]] 2.63&Aring;' scene=''>
+
<StructureSection load='4nre' size='340' side='right'caption='[[4nre]], [[Resolution|resolution]] 2.63&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4nre]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NRE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NRE FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4nre]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NRE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NRE FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.63&#8491;</td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ALOX15B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4nre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nre OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nre RCSB], [http://www.ebi.ac.uk/pdbsum/4nre PDBsum]</span></td></tr>
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4nre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nre OCA], [https://pdbe.org/4nre PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nre RCSB], [https://www.ebi.ac.uk/pdbsum/4nre PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nre ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/LX15B_HUMAN LX15B_HUMAN]] Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. Converts arachidonic acid to 15S-hydroperoxyeicosatetraenoic acid/(15S)-HPETE. Also acts on linoleic acid to produce 13-hydroxyoctadecadienoic acid/13-HPODE. Has no detectable 8S-lipoxygenase activity but reacts with (8S)-HPETE to produce (8S,15S)-diHPETE. May regulate progression through the cell cycle and cell proliferation. May also regulate cytokine secretion by macrophages and therefore play a role in the immune response. May also regulate macrophages differentiation into proatherogenic foam cells.<ref>PMID:11839751</ref> <ref>PMID:10625675</ref> <ref>PMID:12704195</ref> <ref>PMID:16112079</ref> <ref>PMID:18067895</ref> <ref>PMID:22912809</ref>
+
[https://www.uniprot.org/uniprot/LX15B_HUMAN LX15B_HUMAN] Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. Converts arachidonic acid to 15S-hydroperoxyeicosatetraenoic acid/(15S)-HPETE. Also acts on linoleic acid to produce 13-hydroxyoctadecadienoic acid/13-HPODE. Has no detectable 8S-lipoxygenase activity but reacts with (8S)-HPETE to produce (8S,15S)-diHPETE. May regulate progression through the cell cycle and cell proliferation. May also regulate cytokine secretion by macrophages and therefore play a role in the immune response. May also regulate macrophages differentiation into proatherogenic foam cells.<ref>PMID:11839751</ref> <ref>PMID:10625675</ref> <ref>PMID:12704195</ref> <ref>PMID:16112079</ref> <ref>PMID:18067895</ref> <ref>PMID:22912809</ref>
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
Atherosclerosis is associated with chronic inflammation occurring over decades. The enzyme 15-lipoxygenase-2 (15-LOX-2) is highly expressed in large atherosclerotic plaques, and its activity has been linked to the progression of macrophages to the lipid-laden foam cells present in atherosclerotic plaques. We report here the crystal structure of human 15-LOX-2 in complex with an inhibitor that appears to bind as a substrate mimic. 15-LOX-2 contains a long loop, composed of hydrophobic amino acids, which projects from the amino-terminal membrane-binding domain. The loop is flanked by two Ca(2+)-binding sites that confer Ca(2+)-dependent membrane binding. A comparison of the human 15-LOX-2 and 5-LOX structures reveals similarities at the active sites, as well striking differences that can be exploited for design of isoform-selective inhibitors.
+
-
 
+
-
The structure of human 15-lipoxygenase-2 with a substrate mimic.,Kobe MJ, Neau DB, Mitchell CE, Bartlett SG, Newcomer ME J Biol Chem. 2014 Mar 21;289(12):8562-9. doi: 10.1074/jbc.M113.543777. Epub 2014 , Feb 4. PMID:24497644<ref>PMID:24497644</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Human]]
+
[[Category: Homo sapiens]]
-
[[Category: Bartlett, S G]]
+
[[Category: Large Structures]]
-
[[Category: Kobe, M J]]
+
[[Category: Bartlett SG]]
-
[[Category: Mitchell, C E]]
+
[[Category: Kobe MJ]]
-
[[Category: Neau, D B]]
+
[[Category: Mitchell CE]]
-
[[Category: Newcomer, M E]]
+
[[Category: Neau DB]]
-
[[Category: Calcium binding]]
+
[[Category: Newcomer ME]]
-
[[Category: Oxidoreductase]]
+

Current revision

The structure of human 15-lipoxygenase-2 with a substrate mimic

PDB ID 4nre

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4nre"
Personal tools