6ks1

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Current revision (10:41, 22 November 2023) (edit) (undo)
 
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====
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==Crystal structure of the human adiponectin receptor 2==
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<StructureSection load='6ks1' size='340' side='right'caption='[[6ks1]]' scene=''>
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<StructureSection load='6ks1' size='340' side='right'caption='[[6ks1]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6ks1]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3wxw 3wxw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KS1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KS1 FirstGlance]. <br>
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</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=6ks1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ks1 OCA], [http://pdbe.org/6ks1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ks1 RCSB], [http://www.ebi.ac.uk/pdbsum/6ks1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ks1 ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LPX:(2S)-3-{[(R)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-2-HYDROXYPROPYL+HEXADECANOATE'>LPX</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene>, <scene name='pdbligand=OLB:(2S)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLB</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ks1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ks1 OCA], [https://pdbe.org/6ks1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ks1 RCSB], [https://www.ebi.ac.uk/pdbsum/6ks1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ks1 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PAQR2_HUMAN PAQR2_HUMAN] Receptor for ADIPOQ, an essential hormone secreted by adipocytes that regulates glucose and lipid metabolism (PubMed:12802337, PubMed:25855295). Required for normal body fat and glucose homeostasis. ADIPOQ-binding activates a signaling cascade that leads to increased PPARA activity, and ultimately to increased fatty acid oxidation and glucose uptake. Has intermediate affinity for globular and full-length adiponectin. Required for normal revascularization after chronic ischemia caused by severing of blood vessels (By similarity).[UniProtKB:Q8BQS5]<ref>PMID:12802337</ref> <ref>PMID:25855295</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The human adiponectin receptors, AdipoR1 and AdipoR2, are key anti-diabetic molecules. We previously reported the crystal structures of human AdipoR1 and AdipoR2, revealing that their seven transmembrane helices form an internal closed cavity (the closed form). In this study, we determined the crystal structure of the D208A variant AdipoR1, which is fully active with respect to the major downstream signaling. Among the three molecules in the asymmetric unit, two assume the closed form, and the other adopts the open form with large openings in the internal cavity. Between the closed- and open-form structures, helices IV and V are tilted with their intracellular ends shifted by about 4 and 11 A, respectively. Furthermore, we reanalyzed our previous wild-type AdipoR1 diffraction data, and determined a 44:56 mixture of the closed and open forms, respectively. Thus, we have clarified the closed-open interconversion of AdipoR1, which may be relevant to its functional mechanism(s).
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Human adiponectin receptor AdipoR1 assumes closed and open structures.,Tanabe H, Fujii Y, Okada-Iwabu M, Iwabu M, Kano K, Kawana H, Hato M, Nakamura Y, Terada T, Kimura-Someya T, Shirouzu M, Kawano Y, Yamamoto M, Aoki J, Yamauchi T, Kadowaki T, Yokoyama S Commun Biol. 2020 Aug 14;3(1):446. doi: 10.1038/s42003-020-01160-4. PMID:32796916<ref>PMID:32796916</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6ks1" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Antibody 3D structures|Antibody 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Z-disk]]
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[[Category: Mus musculus]]
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[[Category: Fujii Y]]
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[[Category: Hosaka T]]
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[[Category: Iwabu M]]
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[[Category: Kadowaki T]]
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[[Category: Kimura-Someya T]]
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[[Category: Nakamura Y]]
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[[Category: Okada-Iwabu M]]
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[[Category: Shirouzu M]]
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[[Category: Tanabe H]]
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[[Category: Yamauchi T]]
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[[Category: Yokoyama S]]

Current revision

Crystal structure of the human adiponectin receptor 2

PDB ID 6ks1

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