1k0n

From Proteopedia

Revision as of 14:10, 15 February 2008

Chloride Intracellular Channel 1 (CLIC1) complexed with glutathione

Overview

CLIC1 (NCC27) is a member of the highly conserved class of chloride ion, channels that exists 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-A resolution. The, protein is monomeric and structurally homologous to the glutathione, S-transferase 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 (residues 1-90), 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.

About this Structure

1K0N is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of a soluble form of the intracellular chloride ion channel CLIC1 (NCC27) at 1.4-A resolution., Harrop SJ, DeMaere MZ, Fairlie WD, Reztsova T, Valenzuela SM, Mazzanti M, Tonini R, Qiu MR, Jankova L, Warton K, Bauskin AR, Wu WM, Pankhurst S, Campbell TJ, Breit SN, Curmi PM, J Biol Chem. 2001 Nov 30;276(48):44993-5000. Epub 2001 Sep 10. PMID:11551966

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