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Cell signalling

Shared class A GPCR activation path

Zhou Q, Yang D, Wu M, et al. · eLife · 2019

Open access · cc by · source: Europe PMC

Class A GPCRs share a conserved residue-contact rearrangement pathway from ligand pocket to G-protein site.

Study at a glance

Design
Computational / modelling — Residue–residue contact score comparison across inactive and active Class A GPCR structures
N
N=169 · 142 inactive and 27 active structures compared
Population
Class A GPCR crystal/cryo-EM structures
Outcome
Conserved 34-residue-pair activation contact pathway

Structured fields used in claim comparison tables when every cited study has a complete layer.

Key findings

A 34-residue-pair pathway across layers; comparisons used 142 inactive and 27 active structures (p<0.001).

Methodology

Quantified residue–residue contact scores across inactive/active structures and identified conserved switching/repacking contacts.

Limitations

Does not replace ligand-specific pharmacology for every receptor.

How this study connects

Role on claims

Each row is a claim on a concept or method page where this paper supports, challenges, or qualifies the statement. Roles are hand-checked — not a model guess.

  • SupportsCell signallingconcept

    Multiple empirical papers in this library examine cell signalling with mechanistic biological findings.

    Evidence for the claim as stated.

  • SupportsCell signallingconcept

    A 34-residue-pair pathway across layers; comparisons used 142 inactive and 27 active structures (p<0.001).

    Evidence for the claim as stated.

  • SupportsCell signallingconcept

    Systems and scales differ across cell signalling studies (species, tissues, methods), so mechanisms should not be over-generalised.

    Evidence for the claim as stated.

  • SupportsElectron Microscopymethod

    Class A GPCR activation was inferred from residue–residue contact scores across 142 inactive and 27 active structures (p<0.001), yielding a 34-residue-pair pathway across layers. That is comparative structural biology on deposited structures (often crystallography or cryo-EM of isolated receptors), not a trafficking EM study of endosomes, and it does not replace ligand-specific pharmacology.

    Evidence for the claim as stated.

  • SupportsElectron Microscopymethod

    Only the caveolar paper is clearly an ultrastructure-of-a-coat study. GPCR work compares 142 inactive and 27 active deposited structures; APEX2 is proteomics; salmon work is a 30-day transcriptome of fat-cell differentiation; Bt OMV uptake is live light-microscopy trafficking. Calling all five 'electron microscopy papers' overstates shared methods.

    Evidence for the claim as stated.

  • SupportsElectron Microscopymethod

    Resolution targets disagree. Caveolar EM asks about coat stoichiometry (Cavin 1 trimers; exclusion of EHD2/pacsin 2). GPCR contact maps ask about conserved switches across receptors (34 residue pairs). OMV live imaging asks about a 15-minute endocytic route. Those answers cannot substitute for one another.

    Evidence for the claim as stated.

Open questions

Tensions this paper is part of

From concept pages' “where studies disagree.” Disagreement means the same question; scope means different assays, populations, or outcomes.

Related papers in this topic

Same topic cluster — not a recommendation engine.