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.

Student Author(s)

Walter M. Kim

UMMS Affiliation

Graduate School of Biomedical Sciences, MD/PhD Program; Department of Pathology

Publication Date


Document Type


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.

Rights and Permissions

Citation: Biochemistry. 2008 Dec 9;47(49):12942-4.

Related Resources

Link to article in PubMed

PubMed ID