PROSITE documentation PDOC50134Zinc finger TAZ-type profile
Cyclic-AMP response element binding protein (CBP) and the related protein p300 are large nuclear molecules that interact with transcriptional activators and repressors. They belong to a class of protein containing an histone acetyltransferase activity, which suggests a role in chromatin remodeling. They have been implicated in biological function as diverse as cell growth, differentiation, or apoptosis [1].
CBP/P300 proteins contain in their N and C terminal parts the so-called transcriptional adaptor zinc finger (TAZ finger). A TAZ domain is about a 100 amino acid long and shows an internal imperfect triplication of a His-x3-Cys-x12-Cys-x4-Cys module [2]. The binding sites for YY1, E1A and TFIIB in CBP and P300 proteins have been mapped in the region that contain TAZ fingers, suggesting a possible protein-binding function for this domain.
The 3D structure of the TAZ finger has been determined [3]. It folds in a compact globular structure consisting of 4 α helices that coordinates 3 zinc atoms (see <PDB:1F81>). Zinc binding sites are in the loops connecting helices.
This domain has been identified only in proteins belonging to the CBP/P300 family.
The profile we developed covers the entire TAZ domain.
Last update:September 2002 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Giles R.H. Peters D.J. Breuning M.H. |
| Title | Conjunction dysfunction: CBP/p300 in human disease. | |
| Source | Trends Genet. 14:178-183(1998). | |
| PubMed ID | 9613201 |
| 2 | Authors | Ponting C.P. Blake D.J. Davies K.E. Kendrick-Jones J. Winder S.J. |
| Title | ZZ and TAZ: new putative zinc fingers in dystrophin and other proteins. | |
| Source | Trends Biochem. Sci. 21:11-13(1996). | |
| PubMed ID | 8848831 |
| 3 | Authors | De Guzman R.N. Liu H.Y. Martinez-Yamout M. Dyson H.J. Wright P.E. |
| Source | J. Mol. Biol. 303:243-253(2000). |
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