4N5Q

Crystal structure of the N-terminal ankyrin repeat domain of TRPV3

4N5Q の概要

• エントリーDOI: 10.2210/pdb4n5q/pdb
• 分子名称: Transient receptor potential cation channel subfamily V member 3 (2 entities in total)
• 機能のキーワード: ankyrin, channel, protein binding
• 由来する生物種: Mus musculus (mouse)
• 細胞内の位置: Membrane; Multi-pass membrane protein (Probable): Q8K424
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 58689.02

構造登録者

Shi, D.J.,Ye, S.,Cao, X.,Wang, K.W.,Zhang, R. (登録日: 2013-10-10, 公開日: 2014-01-29, 最終更新日: 2024-03-20)

主引用文献

Shi, D.J.,Ye, S.,Cao, X.,Zhang, R.,Wang, K.
Crystal structure of the N-terminal ankyrin repeat domain of TRPV3 reveals unique conformation of finger 3 loop critical for channel function
Protein Cell, 4:942-950, 2013

PubMed Abstract: In all six members of TRPV channel subfamily, there is an ankyrin repeat domain (ARD) in their intracellular N-termini. Ankyrin (ANK) repeat, a common motif with typically 33 residues in each repeat, is primarily involved in protein-protein interactions. Despite the sequence similarity among the ARDs of TRPV channels, the structure of TRPV3-ARD, however, remains unknown. Here, we report the crystal structure of TRPV3-ARD solved at 1.95 Å resolution, which reveals six-ankyrin repeats. While overall structure of TRPV3-ARD is similar to ARDs from other members of TRPV subfamily; it, however, features a noticeable finger 3 loop that bends over and is stabilized by a network of hydrogen bonds and hydrophobic packing, instead of being flexible as seen in known TRPV-ARD structures. Electrophysiological recordings demonstrated that mutating key residues R225, R226, Q255, and F249 of finger 3 loop altered the channel activities and pharmacology. Taken all together, our findings show that TRPV3-ARD with characteristic finger 3 loop likely plays an important role in channel function and pharmacology.

PubMed: 24248473
DOI: 10.1007/s13238-013-3091-0

実験手法

X-RAY DIFFRACTION (1.946 Å)