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Science 10 June 1994:
Vol. 264. no. 5165, pp. 1584 - 1587
DOI: 10.1126/science.7515512
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Articles

Science, Vol 264, Issue 5165, 1584-1587
Copyright © 1994 by American Association for the Advancement of Science

articles

Structure of the equine infectious anemia virus Tat protein

D Willbold, R Rosin-Arbesfeld, H Sticht, R Frank, and P Rosch

Lehrstuhl fur Biopolymere, Universitat Bayreuth, Germany.

Trans-activator (Tat) proteins regulate the transcription of lentiviral DNA in the host cell genome. These RNA binding proteins participate in the life cycle of all known lentiviruses, such as the human immunodeficiency viruses (HIV) or the equine infectious anemia virus (EIAV). The consensus RNA binding motifs [the trans-activation responsive element (TAR)] of HIV-1 as well as EIAV Tat proteins are well characterized. The structure of the 75-amino acid EIAV Tat protein in solution was determined by two- and three-dimensional nuclear magnetic resonance methods and molecular dynamics calculations. The protein structure exhibits a well-defined hydrophobic core of 15 amino acids that serves as a scaffold for two flexible domains corresponding to the NH2- and COOH-terminal regions. The core region is a strictly conserved sequence region among the known Tat proteins. The structural data can be used to explain several of the observed features of Tat proteins.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Detection and Induction of Equine Infectious Anemia Virus-Specific Cytotoxic T-Lymphocyte Responses by Use of Recombinant Retroviral Vectors.
S. M. Lonning, W. Zhang, S. R. Leib, and T. C. McGuire (1999)
J. Virol. 73, 2762-2769
   Abstract »    Full Text »
Structure of Human Parathyroid Hormone 1-37 in Solution.
U. C. Marx, S. Austermann, P. Bayer, K. Adermann, A. Ejchart, H. Sticht, S. Walter, F.-X. Schmid, R. Jaenicke, W.-G. Forssmann, et al. (1995)
J. Biol. Chem. 270, 15194-15202
   Abstract »    Full Text »    PDF »


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