STRUCTURE OF THE EQUINE INFECTIOUS-ANEMIA VIRUS TAT PROTEIN

Citation
D. Willbold et al., STRUCTURE OF THE EQUINE INFECTIOUS-ANEMIA VIRUS TAT PROTEIN, Science, 264(5165), 1994, pp. 1584-1587
Citations number
29
Categorie Soggetti
Multidisciplinary Sciences
Journal title
ISSN journal
00368075
Volume
264
Issue
5165
Year of publication
1994
Pages
1584 - 1587
Database
ISI
SICI code
0036-8075(1994)264:5165<1584:SOTEIV>2.0.ZU;2-D
Abstract
Trans-activator (Tat) proteins regulate the transcription of lentivira l DNA in the host cell genome. These RNA binding proteins participate in the life cycle of all known lentiviruses, such as the human immunod eficiency viruses (HIV) or the equine infectious anemia virus (EIAV). The consensus RNA binding motifs [the trans-activation responsive elem ent (TAR)] of HIV-1 as well as EIAV Tat proteins are well characterize d. The structure of the 75-amino acid EIAV Tat protein in solution was determined by two- and three-dimensional nuclear magnetic resonance m ethods and molecular dynamics calculations. The protein structure exhi bits 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 re gion among the known Tat proteins. The structural data can be used to explain several of the observed features of Tat proteins.