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TitleStructural basis for the tethered peptide activation of adhesion GPCRs.
Journal, issue, pagesNature, Vol. 604, Issue 7907, Page 763-770, Year 2022
Publish dateApr 13, 2022
AuthorsYu-Qi Ping / Peng Xiao / Fan Yang / Ru-Jia Zhao / Sheng-Chao Guo / Xu Yan / Xiang Wu / Chao Zhang / Yan Lu / Fenghui Zhao / Fulai Zhou / Yue-Tong Xi / Wanchao Yin / Feng-Zhen Liu / Dong-Fang He / Dao-Lai Zhang / Zhong-Liang Zhu / Yi Jiang / Lutao Du / Shi-Qing Feng / Torsten Schöneberg / Ines Liebscher / H Eric Xu / Jin-Peng Sun /
PubMed AbstractAdhesion G-protein-coupled receptors (aGPCRs) are important for organogenesis, neurodevelopment, reproduction and other processes. Many aGPCRs are activated by a conserved internal (tethered) agonist ...Adhesion G-protein-coupled receptors (aGPCRs) are important for organogenesis, neurodevelopment, reproduction and other processes. Many aGPCRs are activated by a conserved internal (tethered) agonist sequence known as the Stachel sequence. Here, we report the cryogenic electron microscopy (cryo-EM) structures of two aGPCRs in complex with G: GPR133 and GPR114. The structures indicate that the Stachel sequences of both receptors assume an α-helical-bulge-β-sheet structure and insert into a binding site formed by the transmembrane domain (TMD). A hydrophobic interaction motif (HIM) within the Stachel sequence mediates most of the intramolecular interactions with the TMD. Combined with the cryo-EM structures, biochemical characterization of the HIM motif provides insight into the cross-reactivity and selectivity of the Stachel sequences. Two interconnected mechanisms, the sensing of Stachel sequences by the conserved 'toggle switch' W and the constitution of a hydrogen-bond network formed by Q/Y and the P/VφφG motif (φ indicates a hydrophobic residue), are important in Stachel sequence-mediated receptor activation and G coupling. Notably, this network stabilizes kink formation in TM helices 6 and 7 (TM6 and TM7, respectively). A common G-binding interface is observed between the two aGPCRs, and GPR114 has an extended TM7 that forms unique interactions with G. Our structures reveal the detailed mechanisms of aGPCR activation by Stachel sequences and their G coupling.
External linksNature / PubMed:35418678
MethodsEM (single particle)
Resolution3 - 3.3 Å
Structure data

31232

7ept

EMDB-31232, PDB-7ept:
Structural basis for the tethered peptide activation of adhesion GPCRs
Method: EM (single particle) / Resolution: 3.1 Å

31254

7eq1

EMDB-31254, PDB-7eq1:
GPR114-Gs-scFv16 complex
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-PLM:
PALMITIC ACID

Source
  • homo sapiens (human)
  • bos taurus (cattle)
  • synthetic construct (others)
  • rattus norvegicus (Norway rat)
KeywordsSTRUCTURAL PROTEIN / adhesion GPCR / GPR133 / aGPCR-G protein complex

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