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Papers In Press, published online ahead of print September 10, 2001
Initiative for Biomolecular Structure, University of New South Wales, Sydney, NSW 2052
Corresponding Author: p.curmi{at}unsw.edu.au
CLIC1 (NCC27) is a member of the highly conserved class of chloride ion channels that exist in both soluble and integral membrane forms. Purified CLIC1 can integrate into synthetic lipid bilayers forming a chloride channel with similar properties to those observed in vivo. The structure of the soluble form of CLIC1 has been determined at 1.4 Å resolution. The protein is monomeric, structurally homologous to the GST superfamily and it has a redox-active site resembling glutaredoxin. The structure of the complex of CLIC1 with glutathione shows that glutathione occupies the redox-active site, which is adjacent to an open, elongated slot lined by basic residues. Integration of CLIC1 into the membrane is likely to require a major structural rearrangement, probably of the N-domain, with the putative transmembrane helix arising from residues in the vicinity of the redox-active site. The structure indicates that CLIC1 is likely to be controlled by redox-dependent processes.
J. Biol. Chem, 10.1074/jbc.M107804200
Submitted on August 14, 2001
Revised on September 10, 2001
Accepted on September 7, 2001
Crystal structure of the soluble form of the intracellular chloride Ion channel CLIC1 (NCC27) at 1.4Å resolution
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