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Study · Not a test of the peptide alone · 2024

3 results

Structural basis for hormone recognition and distinctive Gq protein coupling by the kisspeptin receptor.

Shen S, Wang D, Liu H, He X, Cao Y, Chen J, Li S, Cheng X, Xu HE, Duan J

Cell reports26 Jun 2024Cited by 16 (Europe PMC)

Summary

The text of this summary is not shown here, because the article license does not allow reuse. Read it at the source (opens in a new tab)

Text rights: CC BY-NC. Results still quote short attributed sentences.

Results from this study3

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

Studies that did not test the peptide alone3

In this study, Kisspeptin-10 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 Kisspeptin-10.

  1. 01LabNot a test of Kisspeptin-10 aloneIn vitro (cell-free)Mechanism

    Cryo-EM structures of KISS1R bound to kisspeptin‑10 and TAK-448 show key interactions between the peptide ligands and the receptor extracellular loops.

    In plain wordsIn lab structure studies, kisspeptin‑10 and a synthetic analog contact the outer loops of the kisspeptin receptor.

    Outcome
    Not applicablePeptide-receptor interactions in cryo-EM structures
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Reproductive and sexual health

    Source sentences

    Summary
    These structures reveal pivotal interactions between peptide ligands and KISS1R extracellular loops for receptor activation.
    1 context sentence
    Summary · context
    Here, we present cryo-EM structures of KISS1R bound to the endogenous agonist kisspeptin-10 and a synthetic analog TAK-448.

    In this study, Kisspeptin-10 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 Kisspeptin-10.

  2. 02LabNot a test of Kisspeptin-10 aloneIn vitro (cell-free)Mechanism

    Kisspeptin‑10 and TAK-448 show a conserved binding mode at KISS1R.

    In plain wordsIn lab structure studies, kisspeptin‑10 and its synthetic analog bind the receptor in the same way.

    Outcome
    Not applicableBinding mode of kisspeptin-10 and TAK-448
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Reproductive and sexual health

    Source sentences

    Summary
    Both peptides exhibit a conserved binding mode, unveiling their common activation mechanism.
    1 context sentence
    Summary · context
    Here, we present cryo-EM structures of KISS1R bound to the endogenous agonist kisspeptin-10 and a synthetic analog TAK-448.

    In this study, Kisspeptin-10 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 Kisspeptin-10.

  3. 03LabNot a test of Kisspeptin-10 aloneIn vitro (cell-free)Mechanism

    KISS1R shows a 40° angular deviation in its intracellular TM6 region compared with other Gq-coupled receptors.

    In plain wordsIn lab structure studies, the kisspeptin receptor has an unusual inner shape compared with similar receptors.

    Outcome
    Not applicableKISS1R intracellular TM6 angle and Gq coupling
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Reproductive and sexual health

    Source sentences

    Summary
    Intriguingly, KISS1R displays a distinct 40° angular deviation in its intracellular TM6 region compared to other Gq-coupled receptors, enabling distinct interactions with Gq.
    1 context sentence
    Summary · context
    Here, we present cryo-EM structures of KISS1R bound to the endogenous agonist kisspeptin-10 and a synthetic analog TAK-448.

    In this study, Kisspeptin-10 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 Kisspeptin-10.

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

    10 Oct 2026, 09:43 UTC

    Study results updated

  2. Version 1

    9 Oct 2026, 03:04 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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