8IYG

Human neuronal gap junction channel connexin 36

Summary for 8IYG

• Entry DOI: 10.2210/pdb8iyg/pdb
• EMDB information: 35821
• Descriptor: Gap junction delta-2 protein, CHOLESTEROL HEMISUCCINATE, DODECYL-BETA-D-MALTOSIDE (3 entities in total)
• Functional Keywords: channel neuronal connexin dodecamer, membrane protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 12
• Total formula weight: 499882.57

Authors

Mao, W.X.,Chen, S.S. (deposition date: 2023-04-04, release date: 2024-04-10, Last modification date: 2025-07-16)

Primary citation

Mao, W.,Chen, S.
Assembly mechanisms of the neuronal gap junction channel connexin 36 elucidated by Cryo-EM.
Arch.Biochem.Biophys., 754:109959-109959, 2024

PubMed Abstract: Electrical synapses are essential components of neural circuits. Neuronal signal transduction across electrical synapses is primarily mediated by gap junction channels composed of Connexin36 (Cx36), the lack of which causes impaired electrical coupling between certain neurons including cortical interneurons and thalamic reticular nucleus (TRN) neurons. However, the structural basis underlying Cx36 function and assembly remains elusive. Recently, Lee et al. reported cryo-EM structures of Cx36, thus provided first insights of its gating mechanism. Here, we report a consistent cryo-EM structure of Cx36 determined in parallel, and describe unique interactions underpinning its assembly mechanism in complementary to the competing work. In particular, we found non-canonical electrostatic interactions between protomers from opposing hemichannels and a steric complementary site between adjacent protomers within a hemichannel, which together provide a structural explanation for the assembly specificity in homomeric and heteromeric gap junction channels.

PubMed: 38490311
DOI: 10.1016/j.abb.2024.109959

Experimental method

ELECTRON MICROSCOPY (2.69 Å)