Structural studies of the equine infectious anemia virus trans-activator protein.
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.
Willbold
D
D
Lehrstuhl für Biopolymere, Bayreuth, Germany.
Volkmann
A
A
Metzger
A U
AU
Sticht
H
H
Rosin-Arbesfeld
R
R
Gazit
A
A
Yaniv
A
A
Frank
R W
RW
Rösch
P
P
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002460:Cell Line; D002942:Circular Dichroism; D003196:Computer Graphics; D015696:Gene Products, tat / Q000096:biosynthesis / Q000737:chemistry*; D006678:HIV / Q000378:metabolism; D006736:Horses; D006863:Hydrogen-Ion Concentration; D004860:Infectious Anemia Virus, Equine / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D054322:tat Gene Products, Human Immunodeficiency Virus
D015696:Gene Products, tat; D054322:tat Gene Products, Human Immunodeficiency Virus