6krz

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==Crystal structure of the human adiponectin receptor 1 D208A mutant==
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<StructureSection load='6krz' size='340' side='right'caption='[[6krz]]' scene=''>
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<StructureSection load='6krz' size='340' side='right'caption='[[6krz]], [[Resolution|resolution]] 3.05&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'>[[6krz]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KRZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KRZ 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=6krz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6krz OCA], [http://pdbe.org/6krz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6krz RCSB], [http://www.ebi.ac.uk/pdbsum/6krz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6krz 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]] 3.05&#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=OLA:OLEIC+ACID'>OLA</scene>, <scene name='pdbligand=OLB:(2S)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLB</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=6krz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6krz OCA], [https://pdbe.org/6krz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6krz RCSB], [https://www.ebi.ac.uk/pdbsum/6krz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6krz ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PAQR1_HUMAN PAQR1_HUMAN] Receptor for ADIPOQ, an essential hormone secreted by adipocytes that regulates glucose and lipid metabolism (PubMed:25855295, PubMed:12802337). Required for normal glucose and fat homeostasis and for maintaining a normal body weight. ADIPOQ-binding activates a signaling cascade that leads to increased AMPK activity, and ultimately to increased fatty acid oxidation, increased glucose uptake and decreased gluconeogenesis. Has high affinity for globular adiponectin and low affinity for full-length adiponectin (By similarity).[UniProtKB:Q91VH1]<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 6krz" style="background-color:#fffaf0;"></div>
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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: Iwabu M]]
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[[Category: Kadowaki T]]
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[[Category: Okada-Iwabu M]]
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[[Category: Tanabe H]]
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[[Category: Yamauchi T]]
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[[Category: Yokoyama S]]

Revision as of 10:41, 22 November 2023

Crystal structure of the human adiponectin receptor 1 D208A mutant

PDB ID 6krz

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