Probing the pore of ClC-0 by substituted cysteine accessibility method using methane thiosulfonate reagents.

ABSTRACT: ClC channels are a family of protein molecules containing two ion-permeation pores. Although these transmembrane proteins are important for a variety of physiological functions, their molecular operations are only superficially understood. High-resolution X-ray crystallography techniques have recently revealed the structures of two bacterial ClC channels, but whether vertebrate ClC channel pores are similar to those of bacterial homologues is not clear. To study the pore architecture of the Torpedo ClC-0 channel, we employed the substituted-cysteine-accessibility method (SCAM) and used charged methane thiosulfonate (MTS) compounds to modify the introduced cysteine. Several conclusions were derived from this approach. First, the MTS modification pattern from Y512C to E526C in ClC-0, which c

SUBMITTER: Lin CW 

PROVIDER: S-EPMC2229544 | biostudies-literature | 2003 Aug

REPOSITORIES: biostudies-literature