Chloride Intracellular Channel Protein 2: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 9: | Line 9: | ||
Another feature of CLIC proteins distinguishable from other ion channels is that they exist in two different forms: either as soluble globular proteins, or as an integral membrane protein that is incorporated into lipid bilayers and forms ion channels. (X. Meng and al, 2009) These features that are reminiscent of many bacterial pore-forming toxins. (Brett A. Cromer and al, 2007 2) | Another feature of CLIC proteins distinguishable from other ion channels is that they exist in two different forms: either as soluble globular proteins, or as an integral membrane protein that is incorporated into lipid bilayers and forms ion channels. (X. Meng and al, 2009) These features that are reminiscent of many bacterial pore-forming toxins. (Brett A. Cromer and al, 2007 2) | ||
CLIC2 is one of the least characterized CLIC family members. At least two isoforms are known to exist, with the difference being an 18-residue insert occurring immediately after the first β-strand. (Brett A. Cromer and al, 2007 1) It has a molecular weight of 28.4 kDa and a calculated isoelectric point of 5.44. (Wei Mi and al, 2008) Human CLIC2 protein is composed of 247 amino acid residues and is found in many organs, including the spleen, lung, liver, and in both skeletal and cardiac muscles. (X. Meng and al, 2009) The CLIC2 gene locates in the telomeric region of Xq28 and is composed of six coding exons and five introns. Since this region of the X chromosome is closely associated with many hereditary diseases, CLIC2 has thus been proposed as a candidate gene for some genetic disorders linked to Xq28.9. (Wei Mi and al, 2008) Consistent with their high degree of primary structure homology, CLIC2 is similar to CLIC1 and CLIC4 in terms of tertiary structure. Like other members of the CLIC family, CLIC2 can exist as a soluble globular protein, or | CLIC2 is one of the least characterized CLIC family members. At least two isoforms are known to exist, with the difference being an 18-residue insert occurring immediately after the first β-strand. (Brett A. Cromer and al, 2007 1) It has a molecular weight of 28.4 kDa and a calculated isoelectric point of 5.44. (Wei Mi and al, 2008) Human CLIC2 protein is composed of 247 amino acid residues and is found in many organs, including the spleen, lung, liver, and in both skeletal and cardiac muscles. (X. Meng and al, 2009) The CLIC2 gene locates in the telomeric region of Xq28 and is composed of six coding exons and five introns. Since this region of the X chromosome is closely associated with many hereditary diseases, CLIC2 has thus been proposed as a candidate gene for some genetic disorders linked to Xq28.9. (Wei Mi and al, 2008) Consistent with their high degree of primary structure homology, CLIC2 is similar to CLIC1 and CLIC4 in terms of tertiary structure. Like other members of the CLIC family, CLIC2 can exist as a soluble globular protein, or incorporated into a lipid bilayer to form a Cl– channel. (X. Meng and al, 2009 ) | ||
CLIC2 inhibits cardiac ryanodine receptor (RyR) calciumrelease channels, suggesting that CLIC2 may function to regulate calcium release from intracellular stores in the heart and skeletal muscles. (Brett A. Cromer and al, 2007 1) The N-terminal domain of CLIC2 lacks the cysteine equivalent to Cys59 of CLIC1, but contains another cysteine Cys33 that together with the conserved Cys30 (equivalent to Cys24 in CLIC1) forms a CxxC motif similar to glutaredoxin. (Brett A. Cromer and al, 2007 2) | CLIC2 inhibits cardiac ryanodine receptor (RyR) calciumrelease channels, suggesting that CLIC2 may function to regulate calcium release from intracellular stores in the heart and skeletal muscles. (Brett A. Cromer and al, 2007 1) The N-terminal domain of CLIC2 lacks the cysteine equivalent to Cys59 of CLIC1, but contains another cysteine Cys33 that together with the conserved Cys30 (equivalent to Cys24 in CLIC1) forms a CxxC motif similar to glutaredoxin. (Brett A. Cromer and al, 2007 2) | ||
