5IWP

Structure of Transient Receptor Potential (TRP) channel TRPV6 in the presence of calcium

5IWP の概要

• エントリーDOI: 10.2210/pdb5iwp/pdb
• 関連するPDBエントリー: 5IWK 5IWR 5IWT
• 分子名称: Transient receptor potential cation channel subfamily V member 6, CALCIUM ION, 6-(5-METHYL-2-OXO-IMIDAZOLIDIN-4-YL)-HEXANOIC ACID (3 entities in total)
• 機能のキーワード: transport protein
• 由来する生物種: Rattus norvegicus (Rat)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 77482.96

構造登録者

Saotome, K.,Singh, A.K.,Yelshanskaya, M.V.,Sobolevsky, A.I. (登録日: 2016-03-22, 公開日: 2016-06-15, 最終更新日: 2023-09-27)

主引用文献

Saotome, K.,Singh, A.K.,Yelshanskaya, M.V.,Sobolevsky, A.I.
Crystal structure of the epithelial calcium channel TRPV6.
Nature, 534:506-511, 2016

PubMed 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.

PubMed: 27296226
DOI: 10.1038/nature17975

実験手法

X-RAY DIFFRACTION (3.65 Å)