5Y7I

Structure of tilapia fish CLIC2

Summary for 5Y7I

• Entry DOI: 10.2210/pdb5y7i/pdb
• Descriptor: chloride intracellular channel protein 2 (1 entity in total)
• Functional Keywords: glutathione s-transferase structural superfamily, chloride channel activity, transport protein
• Biological source: Oreochromis mossambicus
• Total number of polymer chains: 2
• Total formula weight: 59810.51

Authors

Swaminathan, K.,Zeng, J. (deposition date: 2017-08-17, release date: 2018-03-21, Last modification date: 2024-10-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3 Å)