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TitleHigh-affinity agonists reveal recognition motifs for the MRGPRD GPCR.
Journal, issue, pagesCell Rep, Vol. 43, Issue 12, Page 114942, Year 2024
Publish dateNov 23, 2024
AuthorsChunyu Wang / Yongfeng Liu / Marion Lanier / Adam Yeager / Isha Singh / Ryan H Gumpper / Brian E Krumm / Chelsea DeLeon / Shicheng Zhang / Marcus Boehm / Richard Pittner / Alain Baron / Lisa Dvorak / Corinne Bacon / Brian K Shoichet / Esther Martinborough / Jonathan F Fay / Can Cao / Bryan L Roth /
PubMed AbstractThe human MRGPRD protein is a member of the Mas-related G protein-coupled receptors (MRGPRs) that is involved in the sensing of pain, itch, and other inflammatory stimuli. As with other MRGPRs, ...The human MRGPRD protein is a member of the Mas-related G protein-coupled receptors (MRGPRs) that is involved in the sensing of pain, itch, and other inflammatory stimuli. As with other MRGPRs, MRGPRD is a relatively understudied receptor with few known agonists. The most potent small-molecule agonist of MRGPRD reported so far is β-alanine, with an affinity in the micromole range, which largely restricts its functional study. Here, we report two MRGPRD agonists, EP-2825 and EP-3945, that are approximately 100-fold more potent than β-alanine and determine the structures of MRGPRD-Gq in complex with EP-2825 and EP-3945, respectively. The structures reveal distinct agonist binding modes of MRGPRD and large conformational plasticity of the orthosteric pocket. Collectively, the discovery of high-affinity MRGPRD agonists and their distinct binding modes will facilitate the functional study and the structure-based design of ligands targeting this understudied receptor.
External linksCell Rep / PubMed:39580805
MethodsEM (single particle)
Resolution2.9 - 2.92 Å
Structure data

47113

9dqh

EMDB-47113, PDB-9dqh:
CryoEM structure of Gq-coupled MRGPRD with a new agonist EP-2825
Method: EM (single particle) / Resolution: 2.92 Å

47114

9dqj

EMDB-47114, PDB-9dqj:
CryoEM structure of Gq-coupled MRGPRD with a new agonist EP-3945
Method: EM (single particle) / Resolution: 2.9 Å

Chemicals

PDB-1be2:
LIPID TRANSFER PROTEIN COMPLEXED WITH PALMITATE, NMR, 10 STRUCTURES

PDB-1beq:
INTERACTION BETWEEN PROXIMAL AND DISTALS REGIONS OF CYTOCHROME C PEROXIDASE

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

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