PDBsum entry 6pvq

Transport protein

PDB id: 6pvq

Contents

Protein chains

562 a.a.

518 a.a.

PDB id:

6pvq

Name:

Transport protein

Title:

Cryo-em structure of mouse trpv3-y564a in intermediate state at 37 degrees celsius

Structure:

Transient receptor potential cation channel subfamily v member 3. Chain: a, b, c, d. Synonym: trpv3. Engineered: yes. Mutation: yes

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Gene: trpv3. Expressed in: homo sapiens. Expression_system_taxid: 9606

Authors:

A.K.Singh,L.L.Mcgoldrick,A.I.Sobolevsky

Key ref:

A.K.Singh et al. (2019). Structural basis of temperature sensation by the TRP channel TRPV3. Nat Struct Mol Biol, 26, 994-998. PubMed id: 31636415 DOI: 10.1038/s41594-019-0318-7

Date:

21-Jul-19 Release date: 23-Oct-19

Protein chains

Q8K424  (TRPV3_MOUSE) -  Transient receptor potential cation channel subfamily V member 3 from Mus musculus

Seq: 791 a.a.

Struc: 562 a.a.*

Protein chains

Q8K424  (TRPV3_MOUSE) -  Transient receptor potential cation channel subfamily V member 3 from Mus musculus

Seq: 791 a.a.

Struc: 518 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

DOI no: 10.1038/s41594-019-0318-7

Nat Struct Mol Biol 26:994-998 (2019)

PubMed id: 31636415

Structural basis of temperature sensation by the TRP channel TRPV3.

A.K.Singh, L.L.McGoldrick, L.Demirkhanyan, M.Leslie, E.Zakharian, A.I.Sobolevsky.

ABSTRACT

We present structures of mouse TRPV3 in temperature-dependent open, closed and intermediate states that suggest two-step activation of TRPV3 by heat. During the strongly temperature-dependent first step, sensitization, the channel pore remains closed while S6 helices undergo α-to-π transitions. During the weakly temperature-dependent second step, channel opening, tight association of the S1-S4 and pore domains is stabilized by changes in the carboxy-terminal and linker domains.