|
|
| Line 3: |
Line 3: |
| | <StructureSection load='2wex' size='340' side='right'caption='[[2wex]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='2wex' size='340' side='right'caption='[[2wex]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2wex]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WEX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WEX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2wex]] 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=2WEX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WEX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GYM:(2R)-2,3-DIHYDROXYPROPYL+TETRADECANOATE'>GYM</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]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2wew|2wew]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GYM:(2R)-2,3-DIHYDROXYPROPYL+TETRADECANOATE'>GYM</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=2wex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wex OCA], [https://pdbe.org/2wex PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wex RCSB], [https://www.ebi.ac.uk/pdbsum/2wex PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wex ProSAT]</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=2wex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wex OCA], [https://pdbe.org/2wex PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wex RCSB], [https://www.ebi.ac.uk/pdbsum/2wex PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wex ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/APOM_HUMAN APOM_HUMAN] Probably involved in lipid transport. Can bind sphingosine-1-phosphate, myristic acid, palmitic acid and stearic acid, retinol, all-trans-retinoic acid and 9-cis-retinoic acid.<ref>PMID:17525477</ref> <ref>PMID:19733574</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 31: |
Line 33: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ahnstrom, J]] | + | [[Category: Ahnstrom J]] |
| - | [[Category: Dahlback, B]] | + | [[Category: Dahlback B]] |
| - | [[Category: Egerer-Sieber, C]] | + | [[Category: Egerer-Sieber C]] |
| - | [[Category: Muller, Y A]] | + | [[Category: Muller YA]] |
| - | [[Category: Sevvana, M]] | + | [[Category: Sevvana M]] |
| - | [[Category: Glycoprotein]]
| + | |
| - | [[Category: Hdl]]
| + | |
| - | [[Category: Ligand-binding specificity]]
| + | |
| - | [[Category: Lipid transport]]
| + | |
| - | [[Category: Lipocalin]]
| + | |
| - | [[Category: Lipoprotein]]
| + | |
| - | [[Category: Myristic acid]]
| + | |
| - | [[Category: Transport]]
| + | |
| Structural highlights
Function
APOM_HUMAN Probably involved in lipid transport. Can bind sphingosine-1-phosphate, myristic acid, palmitic acid and stearic acid, retinol, all-trans-retinoic acid and 9-cis-retinoic acid.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Apolipoprotein M (ApoM) is a 25-kDa HDL-associated apolipoprotein and a member of the lipocalin family of proteins. Mature apoM retains its signal peptide, which serves as a lipid anchor attaching apoM to the lipoproteins, thereby keeping it in the circulation. Studies in mice have suggested apoM to be antiatherogenic, but its physiological function is yet unknown. We have now determined the 1.95 A resolution crystal structure of recombinant human apoM expressed in Escherichia coli and made the unexpected discovery that apoM, although refolded from inclusion bodies, was in complex with fatty acids containing 14, 16 or 18 carbon atoms. ApoM displays the typical lipocalin fold characterised by an eight-stranded antiparallel beta-barrel that encloses an internal ligand-binding pocket. The crystal structures of two different complexes provide a detailed picture of the ligand-binding determinants of apoM. Additional fatty acid- and lipid-binding studies with apoM and the mutants apoM(W47F) and apoM(W100F) showed that sphingosine-1-phosphate is able to displace the bound fatty acids and efficiently quenched the intrinsic fluorescence with an IC(50) of 0.90 muM. Whereas the fatty acids bound in the crystal structure could be a mere consequence of recombinant protein production, the observed binding of sphingosine-1-phosphate might provide a key to a better understanding of the physiological function of apoM.
Serendipitous fatty acid binding reveals the structural determinants for ligand recognition in apolipoprotein M.,Sevvana M, Ahnstrom J, Egerer-Sieber C, Lange HA, Dahlback B, Muller YA J Mol Biol. 2009 Nov 6;393(4):920-36. Epub 2009 Sep 4. PMID:19733574[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ahnstrom J, Faber K, Axler O, Dahlback B. Hydrophobic ligand binding properties of the human lipocalin apolipoprotein M. J Lipid Res. 2007 Aug;48(8):1754-62. Epub 2007 May 24. PMID:17525477 doi:10.1194/jlr.M700103-JLR200
- ↑ Sevvana M, Ahnstrom J, Egerer-Sieber C, Lange HA, Dahlback B, Muller YA. Serendipitous fatty acid binding reveals the structural determinants for ligand recognition in apolipoprotein M. J Mol Biol. 2009 Nov 6;393(4):920-36. Epub 2009 Sep 4. PMID:19733574 doi:10.1016/j.jmb.2009.08.071
- ↑ Sevvana M, Ahnstrom J, Egerer-Sieber C, Lange HA, Dahlback B, Muller YA. Serendipitous fatty acid binding reveals the structural determinants for ligand recognition in apolipoprotein M. J Mol Biol. 2009 Nov 6;393(4):920-36. Epub 2009 Sep 4. PMID:19733574 doi:10.1016/j.jmb.2009.08.071
|
