8ibu

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'''Unreleased structure'''
 
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The entry 8ibu is ON HOLD until Paper Publication
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==Cryo-EM structure of the erythromycin-bound motilin receptor-Gq protein complex==
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<StructureSection load='8ibu' size='340' side='right'caption='[[8ibu]], [[Resolution|resolution]] 3.51&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8ibu]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8IBU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IBU FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ERY:ERYTHROMYCIN+A'>ERY</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=8ibu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ibu OCA], [https://pdbe.org/8ibu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ibu RCSB], [https://www.ebi.ac.uk/pdbsum/8ibu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ibu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GBB1_HUMAN GBB1_HUMAN] Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.<ref>PMID:18611381</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Motilin is an endogenous peptide hormone almost exclusively expressed in the human gastrointestinal (GI) tract. It activates the motilin receptor (MTLR), a class A G protein-coupled receptor (GPCR), and stimulates GI motility. To our knowledge, MTLR is the first GPCR reported to be activated by macrolide antibiotics, such as erythromycin. It has attracted extensive attention as a potential drug target for GI disorders. We report two structures of G(q)-coupled human MTLR bound to motilin and erythromycin. Our structures reveal the recognition mechanism of both ligands and explain the specificity of motilin and ghrelin, a related gut peptide hormone, for their respective receptors. These structures also provide the basis for understanding the different recognition modes of erythromycin by MTLR and ribosome. These findings provide a framework for understanding the physiological regulation of MTLR and guiding drug design targeting MTLR for the treatment of GI motility disorders.
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Authors:
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Structural basis for motilin and erythromycin recognition by motilin receptor.,You C, Zhang Y, Xu Y, Xu P, Li Z, Li H, Huang S, Chen Z, Li J, Xu HE, Jiang Y Sci Adv. 2023 Mar 17;9(11):eade9020. doi: 10.1126/sciadv.ade9020. Epub 2023 Mar , 15. PMID:36921049<ref>PMID:36921049</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 8ibu" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Jiang Y]]
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[[Category: Xu HE]]
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[[Category: Xu Y]]
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[[Category: You C]]

Revision as of 20:35, 12 April 2023

Cryo-EM structure of the erythromycin-bound motilin receptor-Gq protein complex

PDB ID 8ibu

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OCA

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