Evolutionarily conserved network properties of intrinsically disordered proteins.

ABSTRACT:

Background

Intrinsically disordered proteins (IDPs) lack a stable tertiary structure in isolation. Remarkably, however, a substantial portion of IDPs undergo disorder-to-order transitions upon binding to their cognate partners. Structural flexibility and binding plasticity enable IDPs to interact with a broad range of partners. However, the broader network properties that could provide additional insights into the functional role of IDPs are not known.

Results

Here, we report the first comprehensive survey of network properties of IDP-induced sub-networks in multiple species from yeast to human. Our results show that IDPs exhibit greater-than-expected modularity and are connected to the rest of the protein interaction network (PIN) via proteins that exhibit the highest betwe

SUBMITTER: Rangarajan N 

PROVIDER: S-EPMC4431869 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature