Three-dimensional structure of a human connexin26 gap junction channel reveals a plug in the vestibule.

ABSTRACT: Connexin molecules form intercellular membrane channels facilitating electronic coupling and the passage of small molecules between adjoining cells. Connexin26 (Cx26) is the second smallest member of the gap junction protein family, and mutations in Cx26 cause certain hereditary human diseases such as skin disorders and hearing loss. Here, we report the electron crystallographic structure of a human Cx26 mutant (M34A). Although crystallization trials used hemichannel preparations, the density map revealed that two hemichannels redocked at their extracellular surfaces into full intercellular channels. These orthorhombic crystals contained two sets of symmetry-related intercellular channels within three lipid bilayers. The 3D map shows a prominent density in the pore of each hemichannel. Thi

SUBMITTER: Oshima A 

PROVIDER: S-EPMC1886001 | biostudies-literature | 2007 Jun

REPOSITORIES: biostudies-literature