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3nkm
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3nkm is ON HOLD Authors: Hiroshi Nishimasu, Ryuichiro Ishitani, Emiko Mihara, Junichi Tkagi, Junken Aoki, Osamu Nureki Description: Mammalian prote...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of mouse autotaxin== | |
| + | <StructureSection load='3nkm' size='340' side='right'caption='[[3nkm]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3nkm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NKM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NKM FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.002Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NKP:(2R)-2-HYDROXY-3-(PHOSPHONOOXY)PROPYL+(9E)-OCTADEC-9-ENOATE'>NKP</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=3nkm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nkm OCA], [https://pdbe.org/3nkm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nkm RCSB], [https://www.ebi.ac.uk/pdbsum/3nkm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nkm ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/ENPP2_MOUSE ENPP2_MOUSE] Note=May contribute to obesity. | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ENPP2_MOUSE ENPP2_MOUSE] Hydrolyzes lysophospholipids to produce lysophosphatidic acid (LPA) in extracellular fluids. Major substrate is lysophosphatidylcholine. Also can act on sphingosylphosphphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility. Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and barely ATP. Involved in several motility-related processes such as angiogenesis and neurite outgrowth. Acts as an angiogenic factor by stimulating migration of smooth muscle cells and microtubule formation. Stimulates migration of melanoma cells, probably via a pertussis toxin-sensitive G protein. May have a role in induction of parturition. Possible involvement in cell proliferation and adipose tissue development. Tumor cell motility-stimulating factor.<ref>PMID:15700135</ref> <ref>PMID:17208043</ref> <ref>PMID:21240269</ref> | ||
| - | + | ==See Also== | |
| - | + | *[[Ectonucleotide pyrophosphatase/phosphodiesterase 3D structures|Ectonucleotide pyrophosphatase/phosphodiesterase 3D structures]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Aoki J]] | ||
| + | [[Category: Ishitani R]] | ||
| + | [[Category: Mihara E]] | ||
| + | [[Category: Nishimasu H]] | ||
| + | [[Category: Nureki O]] | ||
| + | [[Category: Takagi J]] | ||
Current revision
Crystal structure of mouse autotaxin
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Categories: Large Structures | Mus musculus | Aoki J | Ishitani R | Mihara E | Nishimasu H | Nureki O | Takagi J
