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TitleStructure of the human galanin receptor 2 bound to galanin and Gq reveals the basis of ligand specificity and how binding affects the G-protein interface.
Journal, issue, pagesPLoS Biol, Vol. 20, Issue 8, Page e3001714, Year 2022
Publish dateAug 1, 2022
AuthorsYunseok Heo / Naito Ishimoto / Ye-Eun Jeon / Ji-Hye Yun / Mio Ohki / Yuki Anraku / Mina Sasaki / Shunsuke Kita / Hideo Fukuhara / Tatsuya Ikuta / Kouki Kawakami / Asuka Inoue / Katsumi Maenaka / Jeremy R H Tame / Weontae Lee / Sam-Yong Park /
PubMed AbstractGalanin is a neuropeptide expressed in the central and peripheral nervous systems, where it regulates various processes including neuroendocrine release, cognition, and nerve regeneration. Three G- ...Galanin is a neuropeptide expressed in the central and peripheral nervous systems, where it regulates various processes including neuroendocrine release, cognition, and nerve regeneration. Three G-protein coupled receptors (GPCRs) for galanin have been discovered, which is the focus of efforts to treat diseases including Alzheimer's disease, anxiety, and addiction. To understand the basis of the ligand preferences of the receptors and to assist structure-based drug design, we used cryo-electron microscopy (cryo-EM) to solve the molecular structure of GALR2 bound to galanin and a cognate heterotrimeric G-protein, providing a molecular view of the neuropeptide binding site. Mutant proteins were assayed to help reveal the basis of ligand specificity, and structural comparison between the activated GALR2 and inactive hβ2AR was used to relate galanin binding to the movements of transmembrane (TM) helices and the G-protein interface.
External linksPLoS Biol / PubMed:35913979 / PubMed Central
MethodsEM (single particle)
Resolution3.11 Å
Structure data

33103

7xbd

EMDB-33103, PDB-7xbd:
Cryo-EM structure of human galanin receptor 2
Method: EM (single particle) / Resolution: 3.11 Å

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsMEMBRANE PROTEIN / GPCR / GALANIN

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