Structural studies of the equine infectious anemia virus trans-activator protein

Dieter Willbold, Andrea Volkmann, Armin U. Metzger, Heinrich Sticht, Rina Rosin-Arbesfeld, Arnona Gazit, Abraham Yaniv, Reiner W. Frank, Paul Rösch

Research output: Contribution to journalArticlepeer-review


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 .

Original languageEnglish
Pages (from-to)45-52
Number of pages8
JournalEuropean Journal of Biochemistry
Issue number1
StatePublished - 1996


  • Conformation
  • Equine infectious anemia virus
  • Human immunodeficiency virus
  • NMR
  • Trans-activator (tat) protein


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