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Study · Not a test of the peptide alone · 2021

1 result

Molecular recognition of an acyl-peptide hormone and activation of ghrelin receptor.

Wang Y, Guo S, Zhuang Y, Yun Y, Xu P, He X, Guo J, Yin W, Xu HE, Xie X, Jiang Y

Nature communications20 Aug 2021Cited by 65 (Europe PMC)

PMID34417468 (opens in a new tab)PMCIDPMC8379176 (opens in a new tab)DOI10.1038/s41467-021-25364-2 (opens in a new tab)PepBankPUB-34417468
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Summary

Ghrelin, also called "the hunger hormone", is a gastric peptide hormone that regulates food intake, body weight, as well as taste sensation, reward, cognition, learning and memory. One unique feature of ghrelin is its acylation, primarily with an octanoic acid, which is essential for its binding and activation of the ghrelin receptor, a G protein-coupled receptor. The multifaceted roles of ghrelin make ghrelin receptor a highly attractive drug target for growth retardation, obesity, and metabolic disorders. Here we present two cryo-electron microscopy structures of Gq-coupled ghrelin receptor bound to ghrelin and a synthetic agonist, GHRP-6. Analysis of these two structures reveals a unique binding pocket for the octanoyl group, which guides the correct positioning of the peptide to initiate the receptor activation. Together with mutational and functional data, our structures define the rules for recognition of the acylated peptide hormone and activation of ghrelin receptor, and provide structural templates to facilitate drug design targeting ghrelin receptor.
CC BYText from Europe PMC. Highlighted sentences are the source of results.

Results from this study1

No result from this study comes from a test of the peptide.

Studies that did not test the peptide alone1

In this study, GHRP-6 was a lab tool or a carrier, part of a mix, or the subject of a lab method. These results are not evidence about taking GHRP-6.

  1. 01LabNot a test of GHRP-6 aloneIn vitro (cell-free)Mechanism

    In lab tests, cryo-electron microscopy resolved a Gq-coupled ghrelin receptor structure bound to GHRP‑6.

    In plain wordsIn lab tests, researchers resolved the structure of GHRP‑6 bound to the ghrelin receptor.

    Peptide
    GHRP-6
    Outcome
    Not applicableReceptor complex structure
    Study

    n: not reported in source

    Gq-coupled ghrelin receptor bound to GHRP-6
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    Here we present two cryo-electron microscopy structures of Gq-coupled ghrelin receptor bound to ghrelin and a synthetic agonist, GHRP-6.

    In this study, GHRP-6 was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking GHRP-6.

AI wrote and checked these results. AI can make mistakes, so check important results against the source.

Version history

PepBank keeps every version of the data on this study. Status changes from Retraction Watch, Europe PMC and Crossref are listed with their source.

  1. Version 2Current

    21 Oct 2026, 15:58 UTC

    Study results updated

  2. Version 1

    9 Oct 2026, 03:13 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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