Crystal structures of human ETB receptor provide mechanistic insight into receptor activation and partial activation View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2018-12

AUTHORS

Wataru Shihoya, Tamaki Izume, Asuka Inoue, Keitaro Yamashita, Francois Marie Ngako Kadji, Kunio Hirata, Junken Aoki, Tomohiro Nishizawa, Osamu Nureki

ABSTRACT

Endothelin receptors (ETA and ETB) are class A GPCRs activated by vasoactive peptide endothelins, and are involved in blood pressure regulation. ETB-selective signalling induces vasorelaxation, and thus selective ETB agonists are expected to be utilized for improved anti-tumour drug delivery and neuroprotection. Here, we report the crystal structures of human ETB receptor in complex with ETB-selective agonist, endothelin-3 and an ETB-selective endothelin analogue IRL1620. The structure of the endothelin-3-bound receptor reveals that the disruption of water-mediated interactions between W6.48 and D2.50 is critical for receptor activation, while these hydrogen-bonding interactions are partially preserved in the IRL1620-bound structure. Consistently, functional analysis reveals the partial agonistic effect of IRL1620. The current findings clarify the detailed molecular mechanism for the coupling between the orthosteric pocket and the G-protein binding, and the partial agonistic effect of IRL1620, thus paving the way for the design of improved agonistic drugs targeting ETB. More... »

PAGES

4711

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41467-018-07094-0

DOI

http://dx.doi.org/10.1038/s41467-018-07094-0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1108043082

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30413709


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