1TIV

STRUCTURAL STUDIES OF HIV-1 TAT PROTEIN

1TIV の概要

• エントリーDOI: 10.2210/pdb1tiv/pdb
• 分子名称: HIV-1 TRANSACTIVATOR PROTEIN (1 entity in total)
• 機能のキーワード: transcription activation
• 由来する生物種: Human immunodeficiency virus 1
• 細胞内の位置: Host nucleus, host nucleolus: P12506
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9785.23

構造登録者

Bayer, P.,Kraft, M.,Frank, R.,Roesch, P. (登録日: 1995-02-14, 公開日: 1995-07-31, 最終更新日: 2024-05-22)

主引用文献

Bayer, P.,Kraft, M.,Ejchart, A.,Westendorp, M.,Frank, R.,Rosch, P.
Structural studies of HIV-1 Tat protein.
J.Mol.Biol., 247:529-535, 1995

PubMed Abstract: Tat (trans-activator) proteins are early RNA binding proteins regulating lentiviral transcription. These proteins are necessary components in the life cycle of all known lentiviruses, such as the human immunodeficiency viruses (HIV) or the equine infectious anemia virus (EIAV). Tat proteins are thus ideal targets for drugs intervening with lentiviral growth. The consensus RNA binding motif (TAR, trans-activation responsive element) of HIV-1 is well characterized. Structural features of the 86 amino acid HIV-1, Zaire 2 isolate (HV1Z2) Tat protein in solution were determined by two dimensional (2D) nuclear magnetic resonance (NMR) methods and molecular dynamics (MD) calculations. In general, sequence regions corresponded to structural domains of the protein. It exhibited a hydrophobic core of 16 amino acids and a glutamine-rich domain of 17 amino acids. Part of the NH2 terminus, Val4 to Pro14, was sandwiched between these domains. Two highly flexible domains corresponded to a cysteine-rich and a basic sequence region. The 16 amino acid sequence of the core region is strictly conserved among the known Tat proteins, and the three-dimensional fold of these amino acids of HV1Z2 Tat protein was highly similar to the structure of the corresponding EIAV Tat domain. HV1Z2 Tat protein contained a well defined COOH-terminal Arg-Gly-Asp (RGD) loop similar to the recently determined decorsin RGD loop.

PubMed: 7723010
DOI: 10.1006/jmbi.1995.0158

実験手法

SOLUTION NMR