Ontology highlight
ABSTRACT:
SUBMITTER: Wang Y
PROVIDER: S-EPMC3124363 | biostudies-literature | 2011 Apr
REPOSITORIES: biostudies-literature
Wang Yuefeng Y Fisher John C JC Mathew Rose R Ou Li L Otieno Steve S Sublet Jack J Xiao Limin L Chen Jianhan J Roussel Martine F MF Kriwacki Richard W RW
Nature chemical biology 20110227 4
Traditionally, well-defined three-dimensional structure has been thought to be essential for protein function. However, myriad biological functions are performed by highly dynamic, intrinsically disordered proteins (IDPs). IDPs often fold upon binding their biological targets and frequently show 'binding diversity' by targeting multiple ligands. We sought to understand the physical basis of IDP binding diversity and report here that the cyclin-dependent kinase (Cdk) inhibitor p21(Cip1) adaptivel ...[more]