Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 54, Issue -, Pages 10-18Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2018.09.007
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Funding
- French Agence Nationale de la Recherche through ANR JCJC NMRSignal
- French Agence Nationale de la Recherche through ANR T-ERC MAPKassembly
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Advances in characterizing complexes of intrinsically disordered proteins (IDPs) have led to the discovery of a remarkably diverse interaction landscape that includes folding upon -binding, highly dynamic complexes, multivalent interactions as well as regulatory switches controlled by post translational modifications. Nuclear magnetic resonance (NMR) spectroscopy has in recent years made significant contributions to this field by describing the binding mechanisms and mapping conformational dynamics on multiple time scales. Importantly, this progress has been associated with specific methodological developments in NMR, for example in exchange techniques, allowing challenging biological systems to be studied at atomic resolution. In general, the level of dynamics observed in IDP complexes does not correlate with binding affinities, demonstrating the intricate relationship between conformational dynamics and IDP regulatory function.
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