Molecular simulations integrated with experiments for probing the interaction dynamics and binding mechanisms of intrinsically disordered proteins

Curr Opin Struct Biol. 2023 Dec 19;84:102756. doi: 10.1016/j.sbi.2023.102756. Online ahead of print.ABSTRACTIntrinsically disordered proteins (IDPs) exploit their plasticity to deploy a rich panoply of soft interactions and binding phenomena. Advances in tailoring molecular simulations for IDPs combined with experimental cross-validation offer an atomistic view of the mechanisms that control IDP binding, function, and dysfunction. The emerging theme is that unbound IDPs autonomously form transient local structures and self-interactions that determine their binding behavior. Recent results have shed light on whether and how IDPs fold, stay disordered or drive condensation upon binding; how they achieve binding specificity and select among competing partners. The disorder-binding paradigm is now being proactively used by researchers to target IDPs for rational drug design and engineer molecular responsive elements for biosensing applications.PMID:38118365 | DOI:10.1016/j.sbi.2023.102756

Source: Current Opinion in Structural Biology - December 20, 2023 Category: Biology Authors: Catherine Ghosh Suhani Nagpal Victor Mu ñoz Source Type: research