Intrinsic disorder and protein multibinding in domain, terminal, and linker regions.

ABSTRACT: Intrinsic disorder is believed to contribute to the ability of some proteins to interact with multiple partners which is important for protein functional promiscuity and regulation of the cross-talk between pathways. To better understand the mechanisms of molecular recognition through disordered regions, here, we systematically investigate the coupling between disorder and binding within domain families in a structure interaction network and in terminal and inter-domain linker regions. We showed that the canonical domain-domain interaction model should take into account contributions of N- and C-termini and inter-domain linkers, which may form all or part of the binding interfaces. For the majority of proteins, binding interfaces on domain and terminal regions were predicted to be less dis

SUBMITTER: Fong JH 

PROVIDER: S-EPMC2955455 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature