دورية أكاديمية
أعرض في EDS

Cryo-EM structure of the endothelin-1-ET B -G i complex.

التفاصيل البيبلوغرافية
العنوان: Cryo-EM structure of the endothelin-1-ET B -G i complex.
المؤلفون: Sano FK; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan., Akasaka H; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan., Shihoya W; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan., Nureki O; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.
المصدر: ELife [Elife] 2023 Apr 25; Vol. 12. Date of Electronic Publication: 2023 Apr 25.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: eLife Sciences Publications, Ltd Country of Publication: England NLM ID: 101579614 Publication Model: Electronic Cited Medium: Internet ISSN: 2050-084X (Electronic) Linking ISSN: 2050084X NLM ISO Abbreviation: Elife Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Cambridge, UK : eLife Sciences Publications, Ltd., 2012-
مواضيع طبية MeSH: Endothelin-1*/metabolism , Endothelins*/metabolism, Cryoelectron Microscopy ; Receptor, Endothelin B/metabolism ; GTP-Binding Proteins/metabolism
مستخلص: The endothelin ET B receptor is a promiscuous G-protein coupled receptor that is activated by vasoactive peptide endothelins. ET B signaling induces reactive astrocytes in the brain and vasorelaxation in vascular smooth muscle. Consequently, ET B agonists are expected to be drugs for neuroprotection and improved anti-tumor drug delivery. Here, we report the cryo-electron microscopy structure of the endothelin-1-ET B -G i complex at 2.8 Å resolution, with complex assembly stabilized by a newly established method. Comparisons with the inactive ET B receptor structures revealed how endothelin-1 activates the ET B receptor. The NPxxY motif, essential for G-protein activation, is not conserved in ET B , resulting in a unique structural change upon G-protein activation. Compared with other GPCR-G-protein complexes, ET B binds G i in the shallowest position, further expanding the diversity of G-protein binding modes. This structural information will facilitate the elucidation of G-protein activation and the rational design of ET B agonists.
Competing Interests: FS, HA, WS No competing interests declared, ON is a co-founder and scientific advisor for Curreio
(© 2023, Sano et al.)
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فهرسة مساهمة: Keywords: Cryo-EM; Endothelin; GPCR; human; molecular biophysics; structural biology
المشرفين على المادة: 0 (Endothelin-1)
0 (Receptor, Endothelin B)
0 (Endothelins)
EC 3.6.1.- (GTP-Binding Proteins)
تواريخ الأحداث: Date Created: 20230425 Date Completed: 20230426 Latest Revision: 20230513
رمز التحديث: 20240829
مُعرف محوري في PubMed: PMC10129325
DOI: 10.7554/eLife.85821
PMID: 37096326
قاعدة البيانات: MEDLINE
الوصف
تدمد:2050-084X
DOI:10.7554/eLife.85821