HIGHLIGHTS
- What: The authors show that mutating K125 to glutamate mimicking the negative charge of carbamylation causes Cx26 GJCs to be constitutively closed. The authors show that the structure with the K125E mutation matches the more closed conformation of the protein.
- Who: About eLife`s process and collaborators from the School of Life Sciences, University of Warwick, Gibbet Hill Road, Coventry, AL, UK • Leicester Institute of Road, Leicester, HB, UK have published the research work: Structures of wild-type and a constitutively closed mutant of connexin26 shed light on channel regulation by CO, in the Journal . . .
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