Activation mechanism of endothelin ETB receptor by endothelin-1 View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2016-09

AUTHORS

Wataru Shihoya, Tomohiro Nishizawa, Akiko Okuta, Kazutoshi Tani, Naoshi Dohmae, Yoshinori Fujiyoshi, Osamu Nureki, Tomoko Doi

ABSTRACT

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. More... »

PAGES

363

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nature19319

DOI

http://dx.doi.org/10.1038/nature19319

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1049411693

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27595334


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