Tryptophan Scanning Reveals Dense Packing of Connexin Transmembrane Domains in Gap Junction Channels Composed of Connexin32

Tryptophan was substituted for residues in all four transmembrane domains of connexin32. Function was assayed using dual cell two-electrode voltage clamp after expression in Xenopus oocytes. Tryptophan substitution was poorly tolerated in all domains, with the greatest impact in TM1 and TM4. For ins...

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Publicado en:J Biol Chem
Autores principales: Brennan, Matthew J., Karcz, Jennifer, Vaughn, Nicholas R., Woolwine-Cunningham, Yvonne, DePriest, Adam D., Escalona, Yerko, Perez-Acle, Tomas, Skerrett, I. Martha
Formato: Artigo
Lenguaje:Inglês
Publicado: American Society for Biochemistry and Molecular Biology 2015
Materias:
Protein Structure and Folding
Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC4498046/
https://ncbi.nlm.nih.gov/pubmed/25969535
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M115.650747
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