Achieving peptide binding specificity and promiscuity by loops: case of the forkhead-associated domain.

ABSTRACT: The regulation of a series of cellular events requires specific protein-protein interactions, which are usually mediated by modular domains to precisely select a particular sequence from diverse partners. However, most signaling domains can bind to more than one peptide sequence. How do proteins create promiscuity from precision? Moreover, these complex interactions typically occur at the interface of a well-defined secondary structure, α helix and β sheet. However, the molecular recognition primarily controlled by loop architecture is not fully understood. To gain a deep understanding of binding selectivity and promiscuity by the conformation of loops, we chose the forkhead-associated (FHA) domain as our model system. The domain can bind to diverse peptides via various loops but only inte

SUBMITTER: Huang YM 

PROVIDER: S-EPMC4037201 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature