5Y7I

Structure of tilapia fish CLIC2

5Y7I の概要

• エントリーDOI: 10.2210/pdb5y7i/pdb
• 分子名称: chloride intracellular channel protein 2 (1 entity in total)
• 機能のキーワード: glutathione s-transferase structural superfamily, chloride channel activity, transport protein
• 由来する生物種: Oreochromis mossambicus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59810.51

構造登録者

Swaminathan, K.,Zeng, J. (登録日: 2017-08-17, 公開日: 2018-03-21, 最終更新日: 2024-10-23)

主引用文献

Zeng, J.,Li, Z.,Lui, E.Y.,Lam, S.H.,Swaminathan, K.
Tilapia and human CLIC2 structures are highly conserved.
Biochem. Biophys. Res. Commun., 495:1752-1757, 2018

PubMed Abstract: Chloride intracellular channels (CLICs) exist in soluble and membrane bound forms. We have determined the crystal structure of soluble Clic2 from the euryhaline teleost fish Oreochromis mossambicus. Structural comparison of tilapia and human CLIC2 with other CLICs shows that these proteins are highly conserved. We have also compared the expression levels of clic2 in selected osmoregulatory organs of tilapia, acclimated to freshwater, seawater and hypersaline water. Structural conservation of vertebrate CLICs implies that they might play conserved roles. Also, tissue-specific responsiveness of clic2 suggests that it might be involved in iono-osmoregulation under extreme conditions in tilapia.

PubMed: 29198705
DOI: 10.1016/j.bbrc.2017.11.189

実験手法

X-RAY DIFFRACTION (3 Å)