A Gly-zipper motif mediates homodimerization of the transmembrane domain of the mitochondrial kinase ADCK3.

ABSTRACT: Interactions between α-helices within the hydrophobic environment of lipid bilayers are integral to the folding and function of transmembrane proteins; however, the major forces that mediate these interactions remain debated, and our ability to predict these interactions is still largely untested. We recently demonstrated that the frequent transmembrane association motif GASright, the GxxxG-containing fold of the glycophorin A dimer, is optimal for the formation of extended networks of Cα-H hydrogen bonds, supporting the hypothesis that these bonds are major contributors to association. We also found that optimization of Cα-H hydrogen bonding and interhelical packing is sufficient to computationally predict the structure of known GASright dimers at near atomic level. Here, we demonstrate t

SUBMITTER: Khadria AS 

PROVIDER: S-EPMC4195374 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature