1K5K

Homonuclear 1H Nuclear Magnetic Resonance Assignment and Structural Characterization of HIV-1 Tat Mal Protein

1K5K の概要

• エントリーDOI: 10.2210/pdb1k5k/pdb
• 関連するPDBエントリー: 1JFW
• 分子名称: TAT protein (1 entity in total)
• 機能のキーワード: hiv-1, tat, regulatory protein, african variant, nmr., transcription
• 細胞内の位置: Host nucleus, host nucleolus: P04613
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10056.46

構造登録者

Gregoire, C.,Peloponese, J.M.,Esquieu, D.,Opi, S.,Campbell, G.,Solomiac, M.,Lebrun, E.,Lebreton, J.,Loret, E.P. (登録日: 2001-10-11, 公開日: 2002-06-19, 最終更新日: 2024-05-22)

主引用文献

Gregoire, C.,Peloponese Jr., J.M.,Esquieu, D.,Opi, S.,Campbell, G.,Solomiac, M.,Lebrun, E.,Lebreton, J.,Loret, E.P.
Homonuclear (1)H-NMR assignment and structural characterization of human immunodeficiency virus type 1 Tat Mal protein.
Biopolymers, 62:324-335, 2001

PubMed Abstract: The transacting transcriptional activator (Tat) is a viral protein essential for activation of the human immunodeficiency virus (HIV) genes, and it plays an important role in HIV induced immunodeficiency. We report the NMR structural characterization of the active Tat Mal variant that belongs to a highly virulent D-subtype HIV type-1 (HIV-1) strain (Mal) found mainly in Africa. A full Tat Mal protein (87 residues) is synthesized. This synthetic protein is active in a transactivation assay with HeLa cells infected with the HIV long terminal repeated noncoding sequences of the HIV-1 provirus (LTR) lac Z gene. Homonuclear (1)H-NMR spectra allows the sequential assignment of the Tat Mal spin systems. Simulating annealing generates 20 conformers with similar folding. The geometry of the mean structure is optimized with energy minimization to obtain a final structure. As the European variant (Tat Bru) the N-terminal region of Tat Mal constitutes the core, and there is a hydrophobic pocket composed of the conserved Trp 11 interacting with several aromatic residues. The two functional regions of Tat (basic and the cysteine-rich regions) are well exposed to the solvent. A short alpha-helix is observed in region V adjacent to the basic region. This alpha helix induces local structural variations compared to the NMR structure of Tat Bru, and it brings the cysteine-rich and basic regions closer. This study suggests that similar folding exists among Tat variants.

PubMed: 11857271
DOI: 10.1002/bip.10000

実験手法

SOLUTION NMR