3J5P

Structure of TRPV1 ion channel determined by single particle electron cryo-microscopy

Summary for 3J5P

• Entry DOI: 10.2210/pdb3j5p/pdb
• Related: 3J5Q 3J5R
• EMDB information: 5776 5777 5778
• Descriptor: Transient receptor potential cation channel subfamily V member 1 (1 entity in total)
• Functional Keywords: trpv1 channel, transport protein
• Biological source: Rattus norvegicus (rat)
• Total number of polymer chains: 4
• Total formula weight: 272968.62

Authors

Liao, M.,Cao, E.,Julius, D.,Cheng, Y. (deposition date: 2013-10-28, release date: 2013-12-04, Last modification date: 2024-02-21)

Primary citation

Liao, M.,Cao, E.,Julius, D.,Cheng, Y.
Structure of the TRPV1 ion channel determined by electron cryo-microscopy.
Nature, 504:107-112, 2013

PubMed 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.

PubMed: 24305160
DOI: 10.1038/nature12822

Experimental method

ELECTRON MICROSCOPY (3.275 Å)