Open AccessStructural Studies of the Equine Infectious Anemia Virus trans ‐Activator Protein
Author(s) -
Willbold Dieter,
Volkmann Andrea,
Metzger Armin U.,
Sticht Heinrich,
RosinArbesfeld Rina,
Gazit Ara,
Yaniv Abraham,
Frank Rainer W.,
Rösch Paul
Publication year - 1996
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1996.0045h.x
Subject(s) - equine infectious anemia , protein tertiary structure , nucleic acid , virology , protein secondary structure , activator (genetics) , virus , chemistry , amino acid , nuclear magnetic resonance spectroscopy , peptide sequence , biology , protein structure , microbiology and biotechnology , gene , biochemistry , stereochemistry
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.