Title
The intrinsically disordered cytoplasmic domain of the T cell receptor zeta chain binds to the nef protein of simian immunodeficiency virus without a disorder-to-order transition.
UMMS Affiliation
Graduate School of Biomedical Sciences, MD/PhD Program; Department of Pathology
Date
12-9-2008
Document Type
Article
Medical Subject Headings
Binding Sites; Cytoplasm; Dimerization; Electrophoresis, Polyacrylamide Gel; Gene Products, nef; Protein Folding; Protein Structure, Tertiary; Receptors, Antigen, T-Cell; Simian immunodeficiency virus
Abstract
Intrinsically disordered proteins are thought to undergo coupled binding and folding upon interaction with their folded partners. In this study, we investigate whether binding of the intrinsically disordered T cell receptor zeta cytoplasmic tail to the well-folded simian immunodeficiency virus Nef core domain is accompanied by a disorder-to-order transition. We show that zeta forms a 1:1 complex with Nef and remains unfolded in the complex. Thus, our findings oppose the generally accepted view of the behavior of intrinsically disordered proteins and provide new evidence of the existence of specific interactions for unfolded protein molecules.
Rights and Permissions
Citation: Biochemistry. 2008 Dec 9;47(49):12942-4.