6ko5

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Current revision (10:38, 22 November 2023) (edit) (undo)
 
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====
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==Complex structure of Ghrelin receptor with Fab==
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<StructureSection load='6ko5' size='340' side='right'caption='[[6ko5]]' scene=''>
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<StructureSection load='6ko5' size='340' side='right'caption='[[6ko5]], [[Resolution|resolution]] 3.30&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'>[[6ko5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli], [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=6KO5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KO5 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=6ko5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ko5 OCA], [http://pdbe.org/6ko5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ko5 RCSB], [http://www.ebi.ac.uk/pdbsum/6ko5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ko5 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]] 3.3&#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=8QX:6-(4-bromanyl-2-fluoranyl-phenoxy)-2-methyl-3-[[(3~{S})-1-propan-2-ylpiperidin-3-yl]methyl]pyrido[3,2-d]pyrimidin-4-one'>8QX</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=6ko5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ko5 OCA], [https://pdbe.org/6ko5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ko5 RCSB], [https://www.ebi.ac.uk/pdbsum/6ko5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ko5 ProSAT]</span></td></tr>
</table>
</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/GHSR_HUMAN GHSR_HUMAN] Short stature due to GHSR deficiency. The disease is caused by variants affecting the gene represented in this entry.
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== Function ==
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[https://www.uniprot.org/uniprot/C562_ECOLX C562_ECOLX] Electron-transport protein of unknown function.[https://www.uniprot.org/uniprot/GHSR_HUMAN GHSR_HUMAN] Receptor for ghrelin, coupled to G-alpha-11 proteins. Stimulates growth hormone secretion. Binds also other growth hormone releasing peptides (GHRP) (e.g. Met-enkephalin and GHRP-6) as well as non-peptide, low molecular weight secretagogues (e.g. L-692,429, MK-0677, adenosine).<ref>PMID:10604470</ref> <ref>PMID:11322507</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Ghrelin is a gastric peptide hormone with important physiological functions. The unique feature of ghrelin is its Serine 3 acyl-modification, which is essential for ghrelin's activity. However, it remains to be elucidated why the acyl-modification of ghrelin is necessary for activity. To address these questions, we solved the crystal structure of the ghrelin receptor bound to antagonist. The ligand-binding pocket of the ghrelin receptor is bifurcated by a salt bridge between E124 and R283. A striking feature of the ligand-binding pocket of the ghrelin receptor is a wide gap (crevasse) between the TM6 and TM7 bundles that is rich in hydrophobic amino acids, including a cluster of phenylalanine residues. Mutagenesis analyses suggest that the interaction between the gap structure and the acyl acid moiety of ghrelin may participate in transforming the ghrelin receptor into an active conformation.
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Structure of an antagonist-bound ghrelin receptor reveals possible ghrelin recognition mode.,Shiimura Y, Horita S, Hamamoto A, Asada H, Hirata K, Tanaka M, Mori K, Uemura T, Kobayashi T, Iwata S, Kojima M Nat Commun. 2020 Aug 19;11(1):4160. doi: 10.1038/s41467-020-17554-1. PMID:32814772<ref>PMID:32814772</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 6ko5" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Escherichia coli]]
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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: Asada H]]
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[[Category: Hirata K]]
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[[Category: Horita S]]
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[[Category: Iwata S]]
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[[Category: Kojima M]]
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[[Category: Shiimura Y]]

Current revision

Complex structure of Ghrelin receptor with Fab

PDB ID 6ko5

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