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Willbold, Dieter ; Volkmann, Andrea ; Metzger, Armin U. ; Sticht, Heinrich ; Rosin-Arbesfeld, Rina ; Gazit, Arnona ; Yaniv, Abraham ; Frank, Rainer W. ; Rösch, Paul:
Structural Studies of the Equine Infectious Anemia Virus trans-activator Protein.
In: European Journal of Biochemistry.
Bd. 240
(1996)
Heft 1
.
- S. 45-52.
ISSN 1432-1033
DOI: https://doi.org/10.1111/j.1432-1033.1996.0045h.x
Abstract
Trans-activator (tat) proteins are necessary components for the completion of the T replication cycle of lentiviruses. The three-dimensional structure of the equine infectious anemia virus (EIAV) tat protein (e-tat) was studied with CD spectroscopy, NMR spectroscopy, and restrained molecular-dynamics calculations. No stable elements of regular secondary structure were detected, but the sequence regions responsible for nucleic acid binding showed helix-forming tendency, e-tat exhibits a flexible tertiary structure, and only the amino acids comprising the core sequence region form a well-defined tertiary fold. The three-dimensional structure allows discussion of biochemical data as well as data from molecular biological investigations of lentiviral tat proteins.