How disordered is my protein and what is its disorder for? A guide through the “dark side” of the protein universe

Philippe Lieutaud , François Ferron , Alexey V Uversky , Lukasz Kurgan , Vladimir N Uversky , Sonia Longhi (1)

1 AFMB - Architecture et fonction des macromolécules biologiques

In the last 2 decades it has become increasingly evident that a large number of proteins are either fully or partially disordered. Intrinsically disordered proteins lack a stable 3D structure, are ubiquitous and fulfill essential biological functions. Their conformational heterogeneity is encoded in their amino acid sequences, thereby allowing intrinsically disordered proteins or regions to be recognized based on properties of these sequences. The identification of disordered regions facilitates the functional annotation of proteins and is instrumental for delineating boundaries of protein domains amenable to structural determination with X-ray crystallization. This article discusses a comprehensive selection of databases and methods currently employed to disseminate experimental and putative annotations of disorder, predict disorder and identify regions involved in induced folding. It also provides a set of detailed instructions that should be followed to perform computational analysis of disorder.

Mots clés: disorder databases and metaservers; induced folding; intrinsic disorder; intrinsically disordered proteins; intrinsically disordered regions; prediction methods; disorder databases and metaservers

Domaines: Sciences du Vivant [q-bio]

Philippe Lieutaud, François Ferron, Alexey V Uversky, Lukasz Kurgan, Vladimir N Uversky, et al.. How disordered is my protein and what is its disorder for? A guide through the “dark side” of the protein universe. Intrinsically Disordered Proteins, 2016, 4 (1), pp.e1259708. ⟨10.1080/21690707.2016.1259708⟩. ⟨hal-03499972⟩