Component

Inhibitory heterotrimeric G protein / Gi, assay-specified subunits

Inhibitory heterotrimeric G protein / Gi, assay-specified subunits. Species, exposure and limitations are retained in each linked claim.

2 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

How nutrients influence it

Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.

How nutrients reach it in more than one step

Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.

Tracing routes…

What it does

Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.

Recorded relationships

What acts on it

  1. Agonist-bound human MT1 was structurally resolved in a Gi signaling complex.

    Human melatonin receptor 1A / MT1 / MTNR1A → Inhibitory heterotrimeric G protein / Gi, assay-specified subunits source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/melatonin-research/35075127.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "08af0c72228d7c72723f238e83eeabef1ca9196833c7e385ed0c75577c97024b", "start_char": 0, "end_char": 1239, "text_sha256": "08af0c72228d7c72723f238e83eeabef1ca9196833c7e385ed0c75577c97024b"}
    experimental_model
    Cryo-EM structures and functional receptor assays
    exposure
    2-iodomelatonin/ramelteon for MT1; ramelteon for MT2
    limitations
    Structures used agonists, not native melatonin in every complex. Receptor structure does not itself prove clinical effects or subtype-selective supplement actions.
    nutrient_topic
    Melatonin research collection; topical membership is not evidence of a direct dietary effect. · Melatonin
    organism
    Human MT1 and MT2 signaling complexes
    plain_language
    The receptor and its signaling partner are separate searchable components.
    primary_references
    [melatonin-p35075127] Structural basis of the ligand binding and signaling mechanism of melatonin receptors. (2022). https://pubmed.ncbi.nlm.nih.gov/35075127/ DOI: 10.1038/s41467-022-28111-3
    tissue_or_cell_type
    Agonist-bound receptor-Gi coupling

    Melatonin: synthesis, receptors, circadian timing and nutrient interactions (2026-09-17) · lines 396–407

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cryo-EM structures and functional receptor assays · source_derived_draft · unverified_draft

    ### melatonin-mt1-gi-structure Agonist-bound human MT1 was structurally resolved in a Gi signaling complex. Condition category: normal nutrient_topic: Melatonin research collection; topical membership is not evidence of a direct dietary effect. plain_language: The receptor and its signaling partner are separate searchable components. organism: Human MT1 and MT2 signaling complexes tissue_or_cell_type: Agonist-bound receptor-Gi coupling experimental_model: Cryo-EM structures and functional receptor assays limitations: Structures used agonists, not native melatonin in every complex. Receptor structure does not itself prove clinical effects or subtype-selective supplement actions. exposure: 2-iodomelatonin/ramelteon for MT1; ramelteon for MT2 evidence_span: {"source_cache": "artifacts/melatonin-research/35075127.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "08af0c72228d7c72723f238e83eeabef1ca9196833c7e385ed0c75577c97024b", "start_char": 0, "end_char": 1239, "text_sha256": "08af0c72228d7c72723f238e83eeabef1ca9196833c7e385ed0c75577c97024b"} [melatonin-p35075127] Structural basis of the ligand binding and signaling mechanism of melatonin receptors. (2022). https://pubmed.ncbi.nlm.nih.gov/35075127/ DOI: 10.1038/s41467-022-28111-3
    Complete structured claim and evidence

  2. Agonist-bound human MT2 was structurally resolved in a Gi signaling complex.

    Human melatonin receptor 1B / MT2 / MTNR1B → Inhibitory heterotrimeric G protein / Gi, assay-specified subunits source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/melatonin-research/35075127.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "08af0c72228d7c72723f238e83eeabef1ca9196833c7e385ed0c75577c97024b", "start_char": 0, "end_char": 1239, "text_sha256": "08af0c72228d7c72723f238e83eeabef1ca9196833c7e385ed0c75577c97024b"}
    experimental_model
    Cryo-EM structures and functional receptor assays
    exposure
    2-iodomelatonin/ramelteon for MT1; ramelteon for MT2
    limitations
    Structures used agonists, not native melatonin in every complex. Receptor structure does not itself prove clinical effects or subtype-selective supplement actions.
    nutrient_topic
    Melatonin research collection; topical membership is not evidence of a direct dietary effect. · Melatonin
    organism
    Human MT1 and MT2 signaling complexes
    plain_language
    The receptor and its signaling partner are separate searchable components.
    primary_references
    [melatonin-p35075127] Structural basis of the ligand binding and signaling mechanism of melatonin receptors. (2022). https://pubmed.ncbi.nlm.nih.gov/35075127/ DOI: 10.1038/s41467-022-28111-3
    tissue_or_cell_type
    Agonist-bound receptor-Gi coupling

    Melatonin: synthesis, receptors, circadian timing and nutrient interactions (2026-09-17) · lines 409–420

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cryo-EM structures and functional receptor assays · source_derived_draft · unverified_draft

    ### melatonin-mt2-gi-structure Agonist-bound human MT2 was structurally resolved in a Gi signaling complex. Condition category: normal nutrient_topic: Melatonin research collection; topical membership is not evidence of a direct dietary effect. plain_language: The receptor and its signaling partner are separate searchable components. organism: Human MT1 and MT2 signaling complexes tissue_or_cell_type: Agonist-bound receptor-Gi coupling experimental_model: Cryo-EM structures and functional receptor assays limitations: Structures used agonists, not native melatonin in every complex. Receptor structure does not itself prove clinical effects or subtype-selective supplement actions. exposure: 2-iodomelatonin/ramelteon for MT1; ramelteon for MT2 evidence_span: {"source_cache": "artifacts/melatonin-research/35075127.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "08af0c72228d7c72723f238e83eeabef1ca9196833c7e385ed0c75577c97024b", "start_char": 0, "end_char": 1239, "text_sha256": "08af0c72228d7c72723f238e83eeabef1ca9196833c7e385ed0c75577c97024b"} [melatonin-p35075127] Structural basis of the ligand binding and signaling mechanism of melatonin receptors. (2022). https://pubmed.ncbi.nlm.nih.gov/35075127/ DOI: 10.1038/s41467-022-28111-3
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards