Referenced in: none

Automatically associated channels: ClIC1 , Slo1

Title: Crystal structure of a soluble form of the intracellular chloride ion channel CLIC1 (NCC27) at 1.4-A resolution.

Authors: S J Harrop, M Z DeMaere, W D Fairlie, T Reztsova, S M Valenzuela, M Mazzanti, R Tonini, M R Qiu, L Jankova, K Warton, A R Bauskin, W M Wu, S Pankhurst, T J Campbell, S N Breit, P M Curmi

Journal, date & volume: J. Biol. Chem., 2001 Nov 30 , 276, 44993-5000

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/11551966

Abstract
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.