Ontology highlight
ABSTRACT:
SUBMITTER: Liu J
PROVIDER: S-EPMC1622844 | biostudies-literature | 2006 Oct
REPOSITORIES: biostudies-literature
Liu Jie J Zheng Qi Q Deng Yiqun Y Cheng Chao-Sheng CS Kallenbach Neville R NR Lu Min M
Proceedings of the National Academy of Sciences of the United States of America 20061009 42
Coiled-coil proteins contain a characteristic seven-residue sequence repeat whose positions are designated a to g. The interacting surface between alpha-helices in a classical coiled coil is formed by interspersing nonpolar side chains at the a and d positions with hydrophilic residues at the flanking e and g positions. To explore how the chemical nature of these core amino acids dictates the overall coiled-coil architecture, we replaced all eight e and g residues in the GCN4 leucine zipper with ...[more]