1k0n: Difference between revisions

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.

[[Category: Bauskin, A R.]]

[[Category: Breit, S N.]]

[[Category: Campbell, T J.]]

[[Category: Curmi, P M.G.]]

[[Category: DeMaere, M Z.]]

[[Category: Fairlie, W D.]]

[[Category: Harrop, S J.]]

[[Category: Qiu, M R.]]

[[Category: Valenzuela, S M.]]

[[Category: Wu, W M.]]

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