Structure of the TRPV1 ion channel determined by electron cryo-microscopy View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2013-12

AUTHORS

Maofu Liao, Erhu Cao, David Julius, Yifan Cheng

ABSTRACT

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. More... »

PAGES

107

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nature12822

DOI

http://dx.doi.org/10.1038/nature12822

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1042852549

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/24305160


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