5glh: Difference between revisions
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==Human endothelin receptor type-B in complex with ET-1== | |||
<StructureSection load='5glh' size='340' side='right'caption='[[5glh]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5glh]] 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=5GLH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GLH FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</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=5glh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5glh OCA], [https://pdbe.org/5glh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5glh RCSB], [https://www.ebi.ac.uk/pdbsum/5glh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5glh ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/EDN1_HUMAN EDN1_HUMAN] Endothelins are endothelium-derived vasoconstrictor peptides. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Endothelin, a 21-amino-acid peptide, participates in various physiological processes, such as regulation of vascular tone, humoral homeostasis, neural crest cell development and neurotransmission. Endothelin and its G-protein-coupled receptor are involved in the development of various diseases, such as pulmonary arterial hypertension, and thus are important therapeutic targets. Here we report crystal structures of human endothelin type B receptor in the ligand-free form and in complex with the endogenous agonist endothelin-1. The structures and mutation analysis reveal the mechanism for the isopeptide selectivity between endothelin-1 and -3. Transmembrane helices 1, 2, 6 and 7 move and envelop the entire endothelin peptide, in a virtually irreversible manner. The agonist-induced conformational changes are propagated to the receptor core and the cytoplasmic G-protein coupling interface, and probably induce conformational flexibility in TM6. A comparison with the M2 muscarinic receptor suggests a shared mechanism for signal transduction in class A G-protein-coupled receptors. | |||
Activation mechanism of endothelin ETB receptor by endothelin-1.,Shihoya W, Nishizawa T, Okuta A, Tani K, Dohmae N, Fujiyoshi Y, Nureki O, Doi T Nature. 2016 Sep 5;537(7620):363-368. doi: 10.1038/nature19319. PMID:27595334<ref>PMID:27595334</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5glh" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Dohmae N]] | |||
[[Category: Doi T]] | |||
[[Category: Fujiyoshi Y]] | |||
[[Category: Nishizawa T]] | |||
[[Category: Nureki O]] | |||
[[Category: Okuta A]] | [[Category: Okuta A]] | ||
[[Category: Shihoya W]] | [[Category: Shihoya W]] | ||
[[Category: Tani K]] | |||
Latest revision as of 04:08, 21 November 2024
Human endothelin receptor type-B in complex with ET-1
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