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.
Graduate School of Biomedical Sciences, MD/PhD Program; Department of Pathology
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
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.
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Citation: Biochemistry. 2008 Dec 9;47(49):12942-4.
Sigalov AB, Kim WM, Saline M, Stern LJ. (2008). 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.. MD/PhD Program. Retrieved from https://escholarship.umassmed.edu/gsbs_mdphd/15