PDBsum entry 5iwk

Transport protein

PDB id: 5iwk

Contents

Protein chain

594 a.a.

Ligands

DTB

Metals

_CA

PDB id:

5iwk

Name:

Transport protein

Title:

Structure of transient receptor potential (trp) channel trpv6

Structure:

Transient receptor potential cation channel subfamily v member 6. Chain: a. Synonym: trpv6,calcium transport protein 1,cat1,epithelial calcium channel 2,ecac2. Engineered: yes. Mutation: yes

Source:

Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: trpv6. Expressed in: homo sapiens. Expression_system_taxid: 9606

Resolution:

3.25Å R-factor: 0.263 R-free: 0.288

Authors:

K.Saotome,A.K.Singh,M.V.Yelshanskaya,A.I.Sobolevsky

Key ref:

K.Saotome et al. (2016). Crystal structure of the epithelial calcium channel TRPV6. Nature, 534, 506-511. PubMed id: 27296226 DOI: 10.1038/nature17975

Date:

22-Mar-16 Release date: 15-Jun-16

Protein chain

Q9R186  (TRPV6_RAT) -  Transient receptor potential cation channel subfamily V member 6 from Rattus norvegicus

Seq: 767 a.a.

Struc: 594 a.a.*

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

DOI no: 10.1038/nature17975

Nature 534:506-511 (2016)

PubMed id: 27296226

Crystal structure of the epithelial calcium channel TRPV6.

K.Saotome, A.K.Singh, M.V.Yelshanskaya, A.I.Sobolevsky.

ABSTRACT

Precise regulation of calcium homeostasis is essential for many physiological functions. The Ca(2+)-selective transient receptor potential (TRP) channels TRPV5 and TRPV6 play vital roles in calcium homeostasis as Ca(2+) uptake channels in epithelial tissues. Detailed structural bases for their assembly and Ca(2+) permeation remain obscure. Here we report the crystal structure of rat TRPV6 at 3.25 Å resolution. The overall architecture of TRPV6 reveals shared and unique features compared with other TRP channels. Intracellular domains engage in extensive interactions to form an intracellular 'skirt' involved in allosteric modulation. In the K(+) channel-like transmembrane domain, Ca(2+) selectivity is determined by direct coordination of Ca(2+) by a ring of aspartate side chains in the selectivity filter. On the basis of crystallographically identified cation-binding sites at the pore axis and extracellular vestibule, we propose a Ca(2+) permeation mechanism. Our results provide a structural foundation for understanding the regulation of epithelial Ca(2+) uptake and its role in pathophysiology.