Intrinsically disordered proteins: emerging interaction specialists

• Published in: Current opinion in structural biology 2015-12, Vol.35, p.49-59
• Main Authors: Tompa, Peter, Schad, Eva, Tantos, Agnes, Kalmar, Lajos
• Format: Article
• Language: English
• Subjects: Amino Acid Motifs; Amino Acid Sequence; Humans; Intrinsically Disordered Proteins - chemistry; Intrinsically Disordered Proteins - metabolism; Molecular Mimicry; Molecular Sequence Data; Protein Interaction Mapping; Protein Processing, Post-Translational
• ISSN: 0959-440X; 1879-033X
• DOI: 10.1016/j.sbi.2015.08.009

•Intrinsically disordered proteins mostly function by molecular recognition.•Post-translational modifications regulate the interactions of IDPs.•Structural disorder can facilitate allosteric regulation.•IDPs are often involved in misfolding and disease.•IDPs can undergo phase transitions to physically organize cell interior. 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’.