Medicine and Health Sciences Commons^™

The Case For Intrinsically Disordered Proteins Playing Contributory Roles In Molecular Recognition Without A Stable 3d Structure, Vladimir N. Uversky, A. Keith Dunker

Molecular Medicine Faculty Publications

The classical ‘lock-and-key’ and ‘induced-fit’ mechanisms for binding both originated in attempts to explain features of enzyme catalysis. For both of these mechanisms and for their recent refinements, enzyme catalysis requires exquisite spatial and electronic complementarity between the substrate and the catalyst. Thus, binding models derived from models originally based on catalysis will be highly biased towards mechanisms that utilize structural complementarity. If mere binding without catalysis is the endpoint, then the structural requirements for the interaction become much more relaxed. Recent observations on specific examples suggest that this relaxation can reach an extreme lack of specific 3D structure, leading …