7CQV

Complex of TRP_CBS1 and Calmodulin_Nlobe

7CQV の概要

• エントリーDOI: 10.2210/pdb7cqv/pdb
• 分子名称: AT15141p, Transient receptor potential protein, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: calmodulin, trp channel, signaling protein
• 由来する生物種: Drosophila melanogaster (Fruit fly); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 27251.76

構造登録者

Shen, Z.S. (登録日: 2020-08-11, 公開日: 2021-06-23, 最終更新日: 2023-11-29)

主引用文献

Chen, W.,Shen, Z.,Asteriti, S.,Chen, Z.,Ye, F.,Sun, Z.,Wan, J.,Montell, C.,Hardie, R.C.,Liu, W.,Zhang, M.
Calmodulin binds to Drosophila TRP with an unexpected mode.
Structure, 29:330-344.e4, 2021

PubMed Abstract: Drosophila TRP is a calcium-permeable cation channel essential for fly visual signal transduction. During phototransduction, Ca mediates both positive and negative feedback regulation on TRP channel activity, possibly via binding to calmodulin (CaM). However, the molecular mechanism underlying Ca modulated CaM/TRP interaction is poorly understood. Here, we discover an unexpected, Ca-dependent binding mode between CaM and TRP. The TRP tail contains two CaM binding sites (CBS1 and CBS2) separated by an ∼70-residue linker. CBS1 binds to the CaM N-lobe and CBS2 recognizes the CaM C-lobe. Structural studies reveal the lobe-specific binding of CaM to CBS1&2. Mutations introduced in both CBS1 and CBS2 eliminated CaM binding in full-length TRP, but surprisingly had no effect on the response to light under physiological conditions, suggesting alternative mechanisms governing Ca-mediated feedback on the channel activity. Finally, we discover that TRPC4, the closest mammalian paralog of Drosophila TRP, adopts a similar CaM binding mode.

PubMed: 33326749
DOI: 10.1016/j.str.2020.11.016

実験手法

X-RAY DIFFRACTION (1.78 Å)