DISOPRED3: precise disordered region predictions with annotated protein-binding activity.

ABSTRACT:

Motivation

A sizeable fraction of eukaryotic proteins contain intrinsically disordered regions (IDRs), which act in unfolded states or by undergoing transitions between structured and unstructured conformations. Over time, sequence-based classifiers of IDRs have become fairly accurate and currently a major challenge is linking IDRs to their biological roles from the molecular to the systems level.

Results

We describe DISOPRED3, which extends its predecessor with new modules to predict IDRs and protein-binding sites within them. Based on recent CASP evaluation results, DISOPRED3 can be regarded as state of the art in the identification of IDRs, and our self-assessment shows that it significantly improves over DISOPRED2 because its predictions are more specific across the whol

SUBMITTER: Jones DT 

PROVIDER: S-EPMC4380029 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature