Secondary structural analysis of the carboxyl-terminal domain from different connexin isoforms.

ABSTRACT: The connexin carboxyl-terminal (CxCT) domain plays a role in the trafficking, localization, and turnover of gap junction channels, as well as the level of gap junction intercellular communication via numerous post-translational modifications and protein-protein interactions. As a key player in the regulation of gap junctions, the CT presents itself as a target for manipulation intended to modify function. Specific to intrinsically disordered proteins, identifying residues whose secondary structure can be manipulated will be critical toward unlocking the therapeutic potential of the CxCT domain. To accomplish this goal, we used biophysical methods to characterize CxCT domains attached to their fourth transmembrane domain (TM4). Circular dichroism and nuclear magnetic resonance were compleme

SUBMITTER: Spagnol G 

PROVIDER: S-EPMC5178975 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature