PDBsum entry 3j5q

Transport protein/toxin

PDB id: 3j5q

Contents

Protein chains

592 a.a.

31 a.a.

PDB id:

3j5q

Name:

Transport protein/toxin

Title:

Structure of trpv1 ion channel in complex with dktx and rtx determined by single particle electron cryo-microscopy

Structure:

Transient receptor potential cation channel subfamily v member 1. Chain: d, b, e, g. Fragment: see remark 999. Synonym: trpv1,capsaicin receptor,osm-9-like trp channel 1,otrpc1, vanilloid receptor 1,vanilloid receptor type 1-like. Engineered: yes. Kappa-theraphotoxin-cg1a 1. Chain: a, c, f, h.

Source:

Rattus norvegicus. Norway rat. Organism_taxid: 10116. Gene: trpv1, vr1, vr1l. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293s gnti. Chilobrachys guangxiensis. Organism_taxid: 278060

Authors:

M.Liao,E.Cao,D.Julius,Y.Cheng

Key ref:

E.Cao et al. (2013). TRPV1 structures in distinct conformations reveal activation mechanisms. Nature, 504, 113-118. PubMed id: 24305161 DOI: 10.1038/nature12823

Date:

28-Oct-13 Release date: 04-Dec-13

Protein chains

O35433  (TRPV1_RAT) -  Transient receptor potential cation channel subfamily V member 1 from Rattus norvegicus

Seq: 838 a.a.

Struc: 592 a.a.*

Protein chains

P0C247  (JZ11A_CHIGU) -  Kappa-theraphotoxin-Cg1a 1 from Chilobrachys guangxiensis

Seq: 86 a.a.

Struc: 31 a.a.

* PDB and UniProt seqs differ at 11 residue positions (black crosses)

DOI no: 10.1038/nature12823

Nature 504:113-118 (2013)

PubMed id: 24305161

TRPV1 structures in distinct conformations reveal activation mechanisms.

E.Cao, M.Liao, Y.Cheng, D.Julius.

ABSTRACT

Transient receptor potential (TRP) channels are polymodal signal detectors that respond to a wide range of physical and chemical stimuli. Elucidating how these channels integrate and convert physiological signals into channel opening is essential to understanding how they regulate cell excitability under normal and pathophysiological conditions. Here we exploit pharmacological probes (a peptide toxin and small vanilloid agonists) to determine structures of two activated states of the capsaicin receptor, TRPV1. A domain (consisting of transmembrane segments 1-4) that moves during activation of voltage-gated channels remains stationary in TRPV1, highlighting differences in gating mechanisms for these structurally related channel superfamilies. TRPV1 opening is associated with major structural rearrangements in the outer pore, including the pore helix and selectivity filter, as well as pronounced dilation of a hydrophobic constriction at the lower gate, suggesting a dual gating mechanism. Allosteric coupling between upper and lower gates may account for rich physiological modulation exhibited by TRPV1 and other TRP channels.