Document Type
Article
Publication Date
2013
Keywords
Cdk, Cyclin-dependent Protein Kinase; IDP, Intrinsically Disordered Protein; IDR, Intrinsically Disordered Region; Pwps, Proteins Waiting for Partners; SF1, Splicing Factor 1; U2AF, U2 Small Nuclear RNA Auxiliary Actor
Digital Object Identifier (DOI)
https://doi.org/10.3410/B5-1
Abstract
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 to molecular recognition with biological consequences that depend not only upon structural and electrostatic complementarity between the binding partners but also upon kinetic, entropic, and generalized electrostatic effects. In addition to this discussion of binding without fixed structure, examples in which unstructured regions carry out important biological functions not involving molecular recognition will also be discussed. Finally, we discuss whether ‘intrinsically disordered protein’ (IDP) represents a useful new concept.
Rights Information
This work is licensed under a Creative Commons Attribution-Noncommercial 3.0 License
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
F1000 Biology Reports, v. 5, art. 1
Scholar Commons Citation
Uversky, Vladimir N. and Dunker, A. Keith, "The Case for Intrinsically Disordered Proteins Playing Contributory Roles in Molecular Recognition Without a Stable 3D Structure" (2013). Molecular Medicine Faculty Publications. 539.
https://digitalcommons.usf.edu/mme_facpub/539
