1F81

SOLUTION STRUCTURE OF THE TAZ2 DOMAIN OF THE TRANSCRIPTIONAL ADAPTOR PROTEIN CBP

1F81 の概要

• エントリーDOI: 10.2210/pdb1f81/pdb
• 分子名称: CREB-BINDING PROTEIN, ZINC ION (2 entities in total)
• 機能のキーワード: zinc finger, taz2, cbp, transcription
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Cytoplasm (By similarity): P45481
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10200.25

構造登録者

De Guzman, R.N.,Liu, H.L.,Martinez-Yamout, M.,Dyson, H.J.,Wright, P.E. (登録日: 2000-06-28, 公開日: 2000-10-18, 最終更新日: 2024-05-22)

主引用文献

De Guzman, R.N.,Liu, H.Y.,Martinez-Yamout, M.,Dyson, H.J.,Wright, P.E.
Solution structure of the TAZ2 (CH3) domain of the transcriptional adaptor protein CBP.
J.Mol.Biol., 303:243-253, 2000

PubMed Abstract: The TAZ2 (CH3) domain of the transcriptional adapter protein CBP has been implicated in direct functional interactions with numerous cellular transcription factors and viral oncoproteins. The solution structure of the TAZ2 domain of murine CBP has been determined by nuclear magnetic resonance (NMR). The protein adopts a novel helical fold stabilized by three zinc ions, each of which is bound to one histidine and three cysteine ligands in HCCC-type motifs. Each zinc-binding site is formed from the carboxy terminus of an alpha-helix, a short loop, and the amino terminus of the next alpha-helix. A peptide derived from the N-terminal transactivation domain of p53 binds specifically to one face of the TAZ2 domain. The close similarities between the TAZ2 and TAZ1 (CH1 domain of CBP/p300) sequences suggest that both domains will adopt similar three-dimensional structures.

PubMed: 11023789
DOI: 10.1006/jmbi.2000.4141

実験手法

SOLUTION NMR