|Title||Intrinsically disordered proteins: emerging interaction specialists.|
|Publication Type||Journal Article|
|Year of Publication||2015|
|Authors||Tompa, P., Schad E., Tantos Á., and Kalmar L.|
|Journal||Curr Opin Struct Biol|
|Date Published||2015 Dec|
|Keywords||Amino 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 Journal||Curr. Opin. Struct. Biol.|
Intrinsically disordered proteins: emerging interaction specialists.