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TitleStructure reveals the activation mechanism of the MC4 receptor to initiate satiation signaling.
Journal, issue, pagesScience, Vol. 372, Issue 6544, Page 808-814, Year 2021
Publish dateMay 21, 2021
AuthorsHadar Israeli / Oksana Degtjarik / Fabrizio Fierro / Vidicha Chunilal / Amandeep Kaur Gill / Nicolas J Roth / Joaquin Botta / Vadivel Prabahar / Yoav Peleg / Li F Chan / Danny Ben-Zvi / Peter J McCormick / Masha Y Niv / Moran Shalev-Benami /
PubMed AbstractObesity is a global epidemic that causes morbidity and impaired quality of life. The melanocortin receptor 4 (MC4R) is at the crux of appetite, energy homeostasis, and body-weight control in the ...Obesity is a global epidemic that causes morbidity and impaired quality of life. The melanocortin receptor 4 (MC4R) is at the crux of appetite, energy homeostasis, and body-weight control in the central nervous system and is a prime target for anti-obesity drugs. Here, we present the cryo-electron microscopy (cryo-EM) structure of the human MC4R-G signaling complex bound to the agonist setmelanotide, a cyclic peptide recently approved for the treatment of obesity. The work reveals the mechanism of MC4R activation, highlighting a molecular switch that initiates satiation signaling. In addition, our findings indicate that calcium (Ca) is required for agonist, but not antagonist, efficacy. These results fill a gap in the understanding of MC4R activation and could guide the design of future weight-management drugs.
External linksScience / PubMed:33858992
MethodsEM (single particle)
Resolution2.97 Å
Structure data

11927

7aue

EMDB-11927, PDB-7aue:
Melanocortin receptor 4 (MC4R) Gs protein complex
Method: EM (single particle) / Resolution: 2.97 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
  • synthetic construct (others)
KeywordsMEMBRANE PROTEIN / MC4R / Melanocortin / Obesity / GPCR / agonist / setmelanotide

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