Intrinsically disordered proteins: emerging interaction specialists.

TitleIntrinsically disordered proteins: emerging interaction specialists.
Publication TypeJournal Article
Year of Publication2015
AuthorsTompa, P., Schad E., Tantos Á., and Kalmar L.
JournalCurr Opin Struct Biol
Date Published2015 Dec
KeywordsAmino Acid Motifs, Amino Acid Sequence, Humans, Intrinsically Disordered Proteins, Molecular Mimicry, Molecular Sequence Data, Protein Interaction Mapping, Protein Processing, Post-Translational

Intrinsically disordered proteins or regions of proteins (IDPs/IDRs) most often function through protein-protein interactions, when they permanently or transiently bind partner molecules with diverse functional consequences. There is a rapid advance in our understanding of the ensuing functional modes, obtained from describing atomic details of individual complexes, proteome-wide studies of interactomes and characterizing loosely assembled hydrogels and tightly packed amyloids. Here we briefly survey the most important recent methodological developments and structural-functional observations, with the aim of increasing the general appreciation of IDPs/IDRs as 'interaction specialists'.

Alternate JournalCurr. Opin. Struct. Biol.
PubMed ID26402567
Research group: