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2yg2

From Proteopedia

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Current revision

Structure of apolioprotein M in complex with Sphingosine 1-Phosphate

Structural highlights

2yg2 is a 2 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 1.7Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

Publication Abstract from PubMed

Protection of the endothelium is provided by circulating sphingosine-1-phosphate (S1P), which maintains vascular integrity. We show that HDL-associated S1P is bound specifically to both human and murine apolipoprotein M (apoM). Thus, isolated human ApoM(+) HDL contained S1P, whereas ApoM(-) HDL did not. Moreover, HDL in Apom(-/-) mice contains no S1P, whereas HDL in transgenic mice overexpressing human apoM has an increased S1P content. The 1.7-A structure of the S1P-human apoM complex reveals that S1P interacts specifically with an amphiphilic pocket in the lipocalin fold of apoM. Human ApoM(+) HDL induced S1P(1) receptor internalization, downstream MAPK and Akt activation, endothelial cell migration, and formation of endothelial adherens junctions, whereas apoM(-) HDL did not. Importantly, lack of S1P in the HDL fraction of Apom(-/-) mice decreased basal endothelial barrier function in lung tissue. Our results demonstrate that apoM, by delivering S1P to the S1P(1) receptor on endothelial cells, is a vasculoprotective constituent of HDL.

Endothelium-protective sphingosine-1-phosphate provided by HDL-associated apolipoprotein M.,Christoffersen C, Obinata H, Kumaraswamy SB, Galvani S, Ahnstrom J, Sevvana M, Egerer-Sieber C, Muller YA, Hla T, Nielsen LB, Dahlback B Proc Natl Acad Sci U S A. 2011 Jun 7;108(23):9613-8. Epub 2011 May 23. PMID:21606363^[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
↑ Christoffersen C, Obinata H, Kumaraswamy SB, Galvani S, Ahnstrom J, Sevvana M, Egerer-Sieber C, Muller YA, Hla T, Nielsen LB, Dahlback B. Endothelium-protective sphingosine-1-phosphate provided by HDL-associated apolipoprotein M. Proc Natl Acad Sci U S A. 2011 Jun 7;108(23):9613-8. Epub 2011 May 23. PMID:21606363 doi:10.1073/pnas.1103187108

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2yg2"

@@ Line 3: / Line 3: @@
 <StructureSection load='2yg2' size='340' side='right'caption='[[2yg2]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2yg2]] is a 2 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=2YG2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2YG2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2yg2]] is a 2 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=2YG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YG2 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=S1P:(2S,3R,4E)-2-AMINO-3-HYDROXYOCTADEC-4-EN-1-YL+DIHYDROGEN+PHOSPHATE'>S1P</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]] 1.7&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wew|2wew]], [[2wex|2wex]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=S1P:(2S,3R,4E)-2-AMINO-3-HYDROXYOCTADEC-4-EN-1-YL+DIHYDROGEN+PHOSPHATE'>S1P</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2yg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yg2 OCA], [http://pdbe.org/2yg2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2yg2 RCSB], [http://www.ebi.ac.uk/pdbsum/2yg2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2yg2 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=2yg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yg2 OCA], [https://pdbe.org/2yg2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yg2 RCSB], [https://www.ebi.ac.uk/pdbsum/2yg2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yg2 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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>
+[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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Ahnstrom, J]]
+[[Category: Ahnstrom J]]
-[[Category: Christoffersen, C]]
+[[Category: Christoffersen C]]
-[[Category: Dahlback, B]]
+[[Category: Dahlback B]]
-[[Category: Egerer-Sieber, C]]
+[[Category: Egerer-Sieber C]]
-[[Category: Galvani, S]]
+[[Category: Galvani S]]
-[[Category: Gowda, S]]
+[[Category: Gowda S]]
-[[Category: Hla, T]]
+[[Category: Hla T]]
-[[Category: Muller, Y A]]
+[[Category: Muller YA]]
-[[Category: Nielsen, L]]
+[[Category: Nielsen L]]
-[[Category: Obinata, H]]
+[[Category: Obinata H]]
-[[Category: Sevvana, M]]
+[[Category: Sevvana M]]
-[[Category: Hdl]]
-[[Category: Lipid transport]]
-[[Category: Lipocalin]]

2yg2

From Proteopedia

Current revision

Structure of apolioprotein M in complex with Sphingosine 1-Phosphate

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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