RGD Reference Report - Structure of the TRPV1 ion channel determined by electron cryo-microscopy. - Rat Genome Database

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Structure of the TRPV1 ion channel determined by electron cryo-microscopy.

Authors: Liao, Maofu  Cao, Erhu  Julius, David  Cheng, Yifan 
Citation: Liao M, etal., Nature. 2013 Dec 5;504(7478):107-12. doi: 10.1038/nature12822.
RGD ID: 13432320
Pubmed: PMID:24305160   (View Abstract at PubMed)
PMCID: PMC4078027   (View Article at PubMed Central)
DOI: DOI:10.1038/nature12822   (Journal Full-text)

Transient receptor potential (TRP) channels are sensors for a wide range of cellular and environmental signals, but elucidating how these channels respond to physical and chemical stimuli has been hampered by a lack of detailed structural information. Here we exploit advances in electron cryo-microscopy to determine the structure of a mammalian TRP channel, TRPV1, at 3.4¿Å resolution, breaking the side-chain resolution barrier for membrane proteins without crystallization. Like voltage-gated channels, TRPV1 exhibits four-fold symmetry around a central ion pathway formed by transmembrane segments 5-6 (S5-S6) and the intervening pore loop, which is flanked by S1-S4 voltage-sensor-like domains. TRPV1 has a wide extracellular 'mouth' with a short selectivity filter. The conserved 'TRP domain' interacts with the S4-S5 linker, consistent with its contribution to allosteric modulation. Subunit organization is facilitated by interactions among cytoplasmic domains, including amino-terminal ankyrin repeats. These observations provide a structural blueprint for understanding unique aspects of TRP channel function.

Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
identical protein binding enablesIPIUniProtKB:O3543313432320PMID:24305160IntAct 

Objects Annotated

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


Additional Information