2ZW3

Structure of the connexin-26 gap junction channel at 3.5 angstrom resolution

Summary for 2ZW3

• Entry DOI: 10.2210/pdb2zw3/pdb
• Descriptor: Gap junction beta-2 protein (1 entity in total)
• Functional Keywords: ion channel, alpha helical membrane channel, two double layered lipid spanning, cellular adhesion, cell junction, cell membrane, deafness, disease mutation, ectodermal dysplasia, gap junction, hearing, ichthyosis, membrane, non-syndromic deafness, palmoplantar keratoderma, polymorphism, transmembrane, cell adhesion
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane; Multi-pass membrane protein: P29033
• Total number of polymer chains: 6
• Total formula weight: 157482.44

Authors

Maeda, S.,Nakagawa, S.,Suga, M.,Yamashita, E.,Oshima, A.,Fujiyoshi, Y.,Tsukihara, T. (deposition date: 2008-12-01, release date: 2009-04-07, Last modification date: 2024-11-06)

Primary citation

Maeda, S.,Nakagawa, S.,Suga, M.,Yamashita, E.,Oshima, A.,Fujiyoshi, Y.,Tsukihara, T.
Structure of the connexin 26 gap junction channel at 3.5 A resolution
Nature, 458:597-602, 2009

PubMed Abstract: Gap junctions consist of arrays of intercellular channels between adjacent cells that permit the exchange of ions and small molecules. Here we report the crystal structure of the gap junction channel formed by human connexin 26 (Cx26, also known as GJB2) at 3.5 A resolution, and discuss structural determinants of solute transport through the channel. The density map showed the two membrane-spanning hemichannels and the arrangement of the four transmembrane helices of the six protomers forming each hemichannel. The hemichannels feature a positively charged cytoplasmic entrance, a funnel, a negatively charged transmembrane pathway, and an extracellular cavity. The pore is narrowed at the funnel, which is formed by the six amino-terminal helices lining the wall of the channel, which thus determines the molecular size restriction at the channel entrance. The structure of the Cx26 gap junction channel also has implications for the gating of the channel by the transjunctional voltage.

PubMed: 19340074
DOI: 10.1038/nature07869

Experimental method

X-RAY DIFFRACTION (3.5 Å)