Ontology highlight
ABSTRACT:
SUBMITTER: Fallas JA
PROVIDER: S-EPMC5367466 | biostudies-literature | 2017 Apr
REPOSITORIES: biostudies-literature
Fallas Jorge A JA Ueda George G Sheffler William W Nguyen Vanessa V McNamara Dan E DE Sankaran Banumathi B Pereira Jose Henrique JH Parmeggiani Fabio F Brunette T J TJ Cascio Duilio D Yeates Todd R TR Zwart Peter P Baker David D
Nature chemistry 20161205 4
Self-assembling cyclic protein homo-oligomers play important roles in biology, and the ability to generate custom homo-oligomeric structures could enable new approaches to probe biological function. Here we report a general approach to design cyclic homo-oligomers that employs a new residue-pair-transform method to assess the designability of a protein-protein interface. This method is sufficiently rapid to enable the systematic enumeration of cyclically docked arrangements of a monomer followed ...[more]