PDBsum entry 5an8

Transport protein

PDB id: 5an8

Contents

Protein chains

586 a.a.

PDB id:

5an8

Name:

Transport protein

Title:

Cryo-electron microscopy structure of rabbit trpv2 ion channel

Structure:

Trpv2. Chain: a, b, c, d. Engineered: yes. Other_details: rabbit trpv2

Source:

Oryctolagus cuniculus. Rabbit. Organism_taxid: 9986. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf9.

Authors:

L.Zubcevic,M.A.J.Herzik,B.C.Chung,G.C.Lander,S.Y.Lee

Key ref:

L.Zubcevic et al. (2016). Cryo-electron microscopy structure of the TRPV2 ion channel. Nat Struct Biol, 23, 180-186. PubMed id: 26779611 DOI: 10.1038/nsmb.3159

Date:

04-Sep-15 Release date: 23-Dec-15

Protein chains

G1SNM3  (G1SNM3_RABIT) -  Transient receptor potential cation channel subfamily V member 2 from Oryctolagus cuniculus

Seq: 817 a.a.

Struc: 586 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

DOI no: 10.1038/nsmb.3159

Nat Struct Biol 23:180-186 (2016)

PubMed id: 26779611

Cryo-electron microscopy structure of the TRPV2 ion channel.

L.Zubcevic, M.A.Herzik, B.C.Chung, Z.Liu, G.C.Lander, S.Y.Lee.

ABSTRACT

Transient receptor potential vanilloid (TRPV) cation channels are polymodal sensors involved in a variety of physiological processes. TRPV2, a member of the TRPV family, is regulated by temperature, by ligands, such as probenecid and cannabinoids, and by lipids. TRPV2 has been implicated in many biological functions, including somatosensation, osmosensation and innate immunity. Here we present the atomic model of rabbit TRPV2 in its putative desensitized state, as determined by cryo-EM at a nominal resolution of ∼4 Å. In the TRPV2 structure, the transmembrane segment 6 (S6), which is involved in gate opening, adopts a conformation different from the one observed in TRPV1. Structural comparisons of TRPV1 and TRPV2 indicate that a rotation of the ankyrin-repeat domain is coupled to pore opening via the TRP domain, and this pore opening can be modulated by rearrangements in the secondary structure of S6.