2O93

Crystal structure of NFAT bound to the HIV-1 LTR tandem kappaB enhancer element

2O93 の概要

• エントリーDOI: 10.2210/pdb2o93/pdb
• 関連するPDBエントリー: 1P7H
• 分子名称: kappaB enhancer element, DNA 25-mer, actor of activated T-cells, cytoplasmic 2 (3 entities in total)
• 機能のキーワード: ig domain; protein-dna complex; double helix, transcription-dna complex, transcription/dna
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q13469
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 118040.56

構造登録者

Bates, D.L.,Chen, L. (登録日: 2006-12-13, 公開日: 2007-06-19, 最終更新日: 2023-08-30)

主引用文献

Bates, D.L.,Barthel, K.K.,Wu, Y.,Kalhor, R.,Stroud, J.C.,Giffin, M.J.,Chen, L.
Crystal structure of NFAT bound to the HIV-1 LTR tandem kappaB enhancer element
Structure, 16:684-694, 2008

PubMed Abstract: The host factor, nuclear factor of activated T-cells (NFAT), regulates the transcription and replication of HIV-1. Here, we have determined the crystal structure of the DNA binding domain of NFAT bound to the HIV-1 long terminal repeat (LTR) tandem kappaB enhancer element at 3.05 A resolution. NFAT binds as a dimer to the upstream kappaB site (Core II), but as a monomer to the 3' end of the downstream kappaB site (Core I). The DNA shows a significant bend near the 5' end of Core I, where a lysine residue from NFAT bound to the 3' end of Core II inserts into the minor groove and seems to cause DNA bases to flip out. Consistent with this structural feature, the 5' end of Core I become hypersensitive to dimethylsulfate in the in vivo footprinting upon transcriptional activation of the HIV-1 LTR. Our studies provide a basis for further investigating the functional mechanisms of NFAT in HIV-1 transcription and replication.

PubMed: 18462673
DOI: 10.1016/j.str.2008.01.020

実験手法

X-RAY DIFFRACTION (3.05 Å)