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
Volume35
Pagination49-59
Date Published2015 Dec
ISSN1879-033X
KeywordsAmino Acid Motifs, Amino Acid Sequence, Humans, Intrinsically Disordered Proteins, Molecular Mimicry, Molecular Sequence Data, Protein Interaction Mapping, Protein Processing, Post-Translational
Abstract

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'.

DOI10.1016/j.sbi.2015.08.009
Alternate JournalCurr. Opin. Struct. Biol.
PubMed ID26402567
Research group: