RGD Reference Report - TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid action. - Rat Genome Database

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TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid action.

Authors: Gao, Y  Cao, E  Julius, D  Cheng, Y 
Citation: Gao Y, etal., Nature. 2016 May 18;534(7607):347-51. doi: 10.1038/nature17964.
RGD ID: 11344330
Pubmed: PMID:27281200   (View Abstract at PubMed)
PMCID: PMC4911334   (View Article at PubMed Central)
DOI: DOI:10.1038/nature17964   (Journal Full-text)

When integral membrane proteins are visualized in detergents or other artificial systems, an important layer of information is lost regarding lipid interactions and their effects on protein structure. This is especially relevant to proteins for which lipids have both structural and regulatory roles. Here we demonstrate the power of combining electron cryo-microscopy with lipid nanodisc technology to ascertain the structure of the rat TRPV1 ion channel in a native bilayer environment. Using this approach, we determined the locations of annular and regulatory lipids and showed that specific phospholipid interactions enhance binding of a spider toxin to TRPV1 through formation of a tripartite complex. Furthermore, phosphatidylinositol lipids occupy the binding site for capsaicin and other vanilloid ligands, suggesting a mechanism whereby chemical or thermal stimuli elicit channel activation by promoting the release of bioactive lipids from a critical allosteric regulatory site.

Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
protein homotetramerization involved_inIDA 11344330PMID:27281200UniProt 

Cellular Component
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
membrane located_inIDA 11344330PMID:27281200UniProt 

Molecular Function

Objects Annotated

Genes (Rattus norvegicus)
Trpv1  (transient receptor potential cation channel, subfamily V, member 1)


Additional Information