A Hendecad Motif Is Preferred for Heterochiral Coiled-Coil Formation.

ABSTRACT: The structural principles that govern interactions between l- and d-peptides are not well understood. Among natural proteins, coiled-coil assemblies formed between or among α-helices are the most regular feature of tertiary and quaternary structures. We recently reported the first high-resolution structures for heterochiral coiled-coil dimers, which represent a starting point for understanding associations of l- and d-polypeptides. These structures were an unexpected outcome from crystallization of a racemic peptide corresponding to the transmembrane domain of the influenza A M2 protein (M2-TM). The reported structures raised the possibility that heterochiral coiled-coil dimers prefer an 11-residue (hendecad) sequence repeat, in contrast to the 7-residue (heptad) sequence repeat that is do

SUBMITTER: Kreitler DF 

PROVIDER: S-EPMC6500429 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature