5y7i
From Proteopedia
Structure of tilapia fish CLIC2
Structural highlights
FunctionPublication Abstract from PubMedChloride 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. Tilapia and human CLIC2 structures are highly conserved.,Zeng J, Li Z, Lui EY, Lam SH, Swaminathan K Biochem Biophys Res Commun. 2018 Jan 8;495(2):1752-1757. doi:, 10.1016/j.bbrc.2017.11.189. Epub 2017 Dec 2. PMID:29198705[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. Loading citation details.. Citations No citations found See AlsoReferences
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