4nre: Difference between revisions

Latest revision as of 12:34, 1 March 2024

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

Structural highlights

4nre is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.63Å
Ligands:	C8E, CA, FE2, GOL, SO4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

References

↑ Tang S, Bhatia B, Maldonado CJ, Yang P, Newman RA, Liu J, Chandra D, Traag J, Klein RD, Fischer SM, Chopra D, Shen J, Zhau HE, Chung LW, Tang DG. Evidence that arachidonate 15-lipoxygenase 2 is a negative cell cycle regulator in normal prostate epithelial cells. J Biol Chem. 2002 May 3;277(18):16189-201. Epub 2002 Feb 11. PMID:11839751 doi:https://dx.doi.org/10.1074/jbc.M111936200
↑ Jisaka M, Kim RB, Boeglin WE, Brash AR. Identification of amino acid determinants of the positional specificity of mouse 8S-lipoxygenase and human 15S-lipoxygenase-2. J Biol Chem. 2000 Jan 14;275(2):1287-93. PMID:10625675
↑ Bhatia B, Maldonado CJ, Tang S, Chandra D, Klein RD, Chopra D, Shappell SB, Yang P, Newman RA, Tang DG. Subcellular localization and tumor-suppressive functions of 15-lipoxygenase 2 (15-LOX2) and its splice variants. J Biol Chem. 2003 Jul 4;278(27):25091-100. Epub 2003 Apr 18. PMID:12704195 doi:https://dx.doi.org/10.1074/jbc.M301920200
↑ Jisaka M, Iwanaga C, Takahashi N, Goto T, Kawada T, Yamamoto T, Ikeda I, Nishimura K, Nagaya T, Fushiki T, Yokota K. Double dioxygenation by mouse 8S-lipoxygenase: specific formation of a potent peroxisome proliferator-activated receptor alpha agonist. Biochem Biophys Res Commun. 2005 Dec 9;338(1):136-43. Epub 2005 Aug 15. PMID:16112079 doi:https://dx.doi.org/10.1016/j.bbrc.2005.08.029
↑ Danielsson KN, Rydberg EK, Ingelsten M, Akyurek LM, Jirholt P, Ullstrom C, Forsberg GB, Boren J, Wiklund O, Hulten LM. 15-Lipoxygenase-2 expression in human macrophages induces chemokine secretion and T cell migration. Atherosclerosis. 2008 Jul;199(1):34-40. Epub 2007 Dec 11. PMID:18067895 doi:https://dx.doi.org/10.1016/j.atherosclerosis.2007.10.027
↑ Magnusson LU, Lundqvist A, Karlsson MN, Skalen K, Levin M, Wiklund O, Boren J, Hulten LM. Arachidonate 15-lipoxygenase type B knockdown leads to reduced lipid accumulation and inflammation in atherosclerosis. PLoS One. 2012;7(8):e43142. doi: 10.1371/journal.pone.0043142. Epub 2012 Aug 17. PMID:22912809 doi:https://dx.doi.org/10.1371/journal.pone.0043142

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Tang S, Bhatia B, Maldonado CJ, Yang P, Newman RA, Liu J, Chandra D, Traag J, Klein RD, Fischer SM, Chopra D, Shen J, Zhau HE, Chung LW, Tang DG. Evidence that arachidonate 15-lipoxygenase 2 is a negative cell cycle regulator in normal prostate epithelial cells. J Biol Chem. 2002 May 3;277(18):16189-201. Epub 2002 Feb 11. PMID:11839751 doi:https://dx.doi.org/10.1074/jbc.M111936200

[2] Jisaka M, Kim RB, Boeglin WE, Brash AR. Identification of amino acid determinants of the positional specificity of mouse 8S-lipoxygenase and human 15S-lipoxygenase-2. J Biol Chem. 2000 Jan 14;275(2):1287-93. PMID:10625675

[3] Bhatia B, Maldonado CJ, Tang S, Chandra D, Klein RD, Chopra D, Shappell SB, Yang P, Newman RA, Tang DG. Subcellular localization and tumor-suppressive functions of 15-lipoxygenase 2 (15-LOX2) and its splice variants. J Biol Chem. 2003 Jul 4;278(27):25091-100. Epub 2003 Apr 18. PMID:12704195 doi:https://dx.doi.org/10.1074/jbc.M301920200

[4] Jisaka M, Iwanaga C, Takahashi N, Goto T, Kawada T, Yamamoto T, Ikeda I, Nishimura K, Nagaya T, Fushiki T, Yokota K. Double dioxygenation by mouse 8S-lipoxygenase: specific formation of a potent peroxisome proliferator-activated receptor alpha agonist. Biochem Biophys Res Commun. 2005 Dec 9;338(1):136-43. Epub 2005 Aug 15. PMID:16112079 doi:https://dx.doi.org/10.1016/j.bbrc.2005.08.029

[5] Danielsson KN, Rydberg EK, Ingelsten M, Akyurek LM, Jirholt P, Ullstrom C, Forsberg GB, Boren J, Wiklund O, Hulten LM. 15-Lipoxygenase-2 expression in human macrophages induces chemokine secretion and T cell migration. Atherosclerosis. 2008 Jul;199(1):34-40. Epub 2007 Dec 11. PMID:18067895 doi:https://dx.doi.org/10.1016/j.atherosclerosis.2007.10.027

[6] Magnusson LU, Lundqvist A, Karlsson MN, Skalen K, Levin M, Wiklund O, Boren J, Hulten LM. Arachidonate 15-lipoxygenase type B knockdown leads to reduced lipid accumulation and inflammation in atherosclerosis. PLoS One. 2012;7(8):e43142. doi: 10.1371/journal.pone.0043142. Epub 2012 Aug 17. PMID:22912809 doi:https://dx.doi.org/10.1371/journal.pone.0043142

[1]

[2]

[3]

[4]

[5]

[6]

@@ Line 1: / Line 1: @@
-{{STRUCTURE_4nre|  PDB=4nre  |  SCENE=  }}
-===The structure of human 15-lipoxygenase-2 with a substrate mimic===
-==Function==
+==The structure of human 15-lipoxygenase-2 with a substrate mimic==
-[[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>
+<StructureSection load='4nre' size='340' side='right'caption='[[4nre]], [[Resolution|resolution]] 2.63&Aring;' scene=''>
+== Structural highlights ==
-==About this Structure==
+<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>
-[[4nre]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NRE OCA].
+</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='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>
-==Reference==
+<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>
-<references group="xtra"/><references/>
+</table>
-[[Category: Bartlett, S G.]]
+== Function ==
-[[Category: Kobe, M J.]]
+[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>
-[[Category: Mitchell, C E.]]
+== References ==
-[[Category: Neau, D B.]]
+<references/>
-[[Category: Newcomer, M E.]]
+__TOC__
-[[Category: Calcium binding]]
+</StructureSection>
-[[Category: Oxidoreductase]]
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Bartlett SG]]
+[[Category: Kobe MJ]]
+[[Category: Mitchell CE]]
+[[Category: Neau DB]]
+[[Category: Newcomer ME]]

4nre: Difference between revisions

Latest revision as of 12:34, 1 March 2024

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

Structural highlights

Function

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools