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• W2170854739 abstract "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." @default.
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• W2170854739 date "1996-08-01" @default.
• W2170854739 modified "2023-09-27" @default.
• W2170854739 title "Structural Studies of the Equine Infectious Anemia Virustrans-Activator Protein" @default.
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• W2170854739 doi "https://doi.org/10.1111/j.1432-1033.1996.0045h.x" @default.
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