The case for intrinsically disordered proteins playing contributory roles in molecular recognition without a stable 3D structure

Vladimir N. Uversky, A. Dunker

Research output: Contribution to journalArticle

57 Citations (Scopus)

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.

Original languageEnglish (US)
Article number1
JournalF1000 Biology Reports
Volume5
Issue number1
DOIs
StatePublished - Jan 11 2013
Externally publishedYes

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Intrinsically Disordered Proteins
Molecular recognition
Catalysis
Static Electricity
Electrostatics
Enzymes
Catalysts
Kinetics
Substrates

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)
  • Neuroscience(all)
  • Pharmacology, Toxicology and Pharmaceutics(all)

Cite this

The case for intrinsically disordered proteins playing contributory roles in molecular recognition without a stable 3D structure. / Uversky, Vladimir N.; Dunker, A.

In: F1000 Biology Reports, Vol. 5, No. 1, 1, 11.01.2013.

Research output: Contribution to journalArticle

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