Prediction of binding sites on intrinsically disordered proteins

Abstract

Russell C. Goodman and Theresa L. Beaty Department of Chemistry and Physics, Le Moyne College, 1419 Salt Springs Road, Syracuse, NY 13214 Introduction Intrinsically disordered proteins (IDPs) are a novel class of proteins that, until over a decade ago, had not been recognized as a functional class of proteins. As opposed to globular and lipidsoluble proteins, IDPs lack a well defined structure. In solution, an IDP adopts an ensemble of conformations; however, when bound to a ligand, an IDP adopts a particular structure with a particular function. Disordered proteins my bind a multitude of ligands, exhibiting what is referred to as binding promiscuity (Uversky 2005). Therefore, rather than adhering strictly to the classical structure-function paradigm associated with globular proteins, IDPs can adopt multiple structures, each possessing a different function.