Structural insight into the activation mechanism of MrgD with heterotrimeric Gi-protein revealed by cryo-EM View Full Text


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Article Info

DATE

2022-07-15

AUTHORS

Shota Suzuki, Momoko Iida, Yoko Hiroaki, Kotaro Tanaka, Akihiro Kawamoto, Takayuki Kato, Atsunori Oshima

ABSTRACT

MrgD, a member of the Mas-related G protein-coupled receptor (MRGPR) family, has high basal activity for Gi activation. It recognizes endogenous ligands, such as β-alanine, and is involved in pain and itch signaling. The lack of a high-resolution structure for MrgD hinders our understanding of whether its activation is ligand-dependent or constitutive. Here, we report two cryo-EM structures of the MrgD-Gi complex in the β-alanine-bound and apo states at 3.1 Å and 2.8 Å resolution, respectively. These structures show that β-alanine is bound to a shallow pocket at the extracellular domains. The extracellular half of the sixth transmembrane helix undergoes a significant movement and is tightly packed into the third transmembrane helix through hydrophobic residues, creating the active form. Our structures demonstrate a structural basis for the characteristic ligand recognition of MrgD. These findings provide a framework to guide drug designs targeting the MrgD receptor. More... »

PAGES

707

References to SciGraph publications

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/s42003-022-03668-3

    DOI

    http://dx.doi.org/10.1038/s42003-022-03668-3

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1149498797

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/35840655


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