TAILIEUCHUNG - Báo cáo khoa học: Crystal structure of the soluble form of the redox-regulated chloride ion channel protein CLIC4

The structure of CLIC4, a member of the CLIC family of putative intracel-lular chloride ion channel proteins, has been determined at A ˚ resolution by X-ray crystallography. The protein is monomeric and it is structurally similar to CLIC1, belonging to the GST fold class. Differences between the structures of CLIC1 and CLIC4 are localized to helix 2 in the glutaredoxin-like N-terminal domain, which has previously been shown to undergo a dra-matic structural change in CLIC1 upon oxidation. | iFEBS Journal Crystal structure of the soluble form of the redox-regulated chloride ion channel protein CLIC4 Dene R. Littler1 2 Nagi N. Assaad1 2 Stephen J. Harrop1 2 Louise J. Brown1 2 3 Greg J. Pankhurst2 Panin I I mi a n Í4 a ri O-lc a ho I Zkn I li la t 5 inholo I Ia77anti4 l larl A Rnrn m a n6 Ram I lol M Rroit2 raoio Luciai II Iviaiie isauei Hguiiai Iviiciieie IVI azzanu iviai N . Deiiyiiian oaiiiuei 1 . DieiL and Paul M. G. Curmi1 2 1 Schoolof Physics University of New South Wales Sydney Australia 2 Centre for Immunology St Vincent s Hospitaland University of New South Wales Sydney Australia 3 Department of Chemistry and Biomolecular Sciences Macquarie University Sydney Australia 4 Department of Cellular and DevelopmentalBiology University of Rome La Sapienza Rome Italy 5 Department of Biochemistry and Molecular Biology Monash University Clayton Victoria Australia 6 Department of BiomedicalSciences Molecular and Cellular Biology Program Ohio University College of Osteopathic Medicine Athens OH USA Keywords CLIC4 glutathione S-transferase ion channel redox regulation X-ray crystallography Correspondence . Curmi Schoolof Physics University of New South Wales Sydney NSW 2052 Australia Fax 61 29385 6060 Tel 61 29385 4552 E-mail Received 29 June 2005 revised 29 July 2005 accepted 9 August 2005 doi The structure of CLIC4 a member of the CLIC family of putative intracellular chloride ion channel proteins has been determined at A resolution by X-ray crystallography. The protein is monomeric and it is structurally similar to CLIC1 belonging to the GST fold class. Differences between the structures of CLIC1 and CLIC4 are localized to helix 2 in the glutaredoxin-like N-terminal domain which has previously been shown to undergo a dramatic structural change in CLIC1 upon oxidation. The structural differences in this region correlate with the sequence differences where the CLIC1 sequence appears to be atypical

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