Multitude of binding modes attainable by intrinsically disordered proteins: a portrait gallery of disorder-based complexes.
Proteins are constantly involved in the multitude of various interactions creating sophisticated networks which define and control all (or almost all) the biological processes taking place in any living organism. Intrinsically disordered proteins or regions play a number of crucial roles in mediating protein interactions. The lack of fixed structure protruding to the high level of intrinsic dynamics and almost unrestricted flexibility at various structure levels, being the major characteristics of intrinsically disordered proteins, provides them with unprecedented advantages over the ordered proteins. The binding modes attainable by disordered proteins are highly diverse, creating a multitude of unusual complexes. Although the majority of studied to date intrinsic disorder-based complexes are ordered or static entities originating due to the global or local disorder-to-order transitions, a new development is the discovery of dynamic complexes in which intrinsically disordered proteins continue to sample an ensemble of rapidly interconverting conformations mostly devoid of structure even in their bound state. The goal of this critical review is to illustrate binding plasticity of intrinsically disordered proteins by representing a portrait gallery of the disorder-based complexes (119 references).
Department of Molecular Medicine, University of South Florida, Tampa, Florida 33612, USA.
Vladimir N
VN
Uversky
D008958:Models, Molecular; D046912:Multiprotein Complexes / Q000737:chemistry*; D011485:Protein Binding; D017434:Protein Structure, Tertiary
D046912:Multiprotein Complexes