1PZU

An asymmetric NFAT1-RHR homodimer on a pseudo-palindromic, Kappa-B site

1PZU の概要

• エントリーDOI: 10.2210/pdb1pzu/pdb
• 関連するPDBエントリー: 1A02
• 分子名称: 5'-D(*TP*TP*GP*AP*GP*GP*AP*AP*TP*TP*TP*CP*CP*A)-3', 5'-D(*AP*AP*TP*GP*GP*AP*AP*AP*TP*TP*CP*CP*TP*C)-3', Nuclear factor of activated T-cells, cytoplasmic 2 (3 entities in total)
• 機能のキーワード: transcription factor, nfat1-rhr homodimer, protein-dna complex, human il8 promoter, 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: 12
• 化学式量合計: 231301.24

構造登録者

Jin, L.,Sliz, P.,Chen, L.,Macian, F.,Rao, A.,Hogan, P.G.,Harrison, S.C. (登録日: 2003-07-14, 公開日: 2003-09-09, 最終更新日: 2024-02-21)

主引用文献

Jin, L.,Sliz, P.,Chen, L.,Macian, F.,Rao, A.,Hogan, P.G.,Harrison, S.C.
An asymmetric NFAT1 dimer on a pseudo-palindromic KB-like DNA site
Nat.Struct.Biol., 10:807-811, 2003

PubMed Abstract: The crystal structure of the NFAT1 Rel homology region (RHR) bound to a pseudo-palindromic DNA site reveals an asymmetric dimer interaction between the RHR-C domains, unrelated to the contact seen in Rel dimers such as NF kappa B. Binding studies with a form of the NFAT1 RHR defective in the dimer contact show loss of cooperativity and demonstrate that the same interaction is present in solution. The structure we have determined may correspond to a functional NFAT binding mode at palindromic sites of genes induced during the anergic response to weak TCR signaling.

PubMed: 12949491
DOI: 10.1038/nsb975

実験手法

X-RAY DIFFRACTION (3.1 Å)