TEA
- Domain
- TEA domain
- Group
- Helix-turn-helix
- PFAM
- PF01285
- Desciption
- The TEA domain is a DNA-binding region of about 66 to 68 amino acids that has been named after the two proteins that originally defined the domain: TEF-1 and AbaA. The TEA domain is located toward the N terminus of eukaryotic transcription factors of the TEA/ATTS family. It shows a three-helix bundle with a homeodomain fold [3, 1]. Two α-helices are nearly anti-parallel and pack on either side of the third one, which is the DNA-recognition helix of the TEA domain. Phosphorylation of one or both of the two conserved serines found on the DNA-binding surface could interfere with DNA-binding activity, by introducing electrostatic repulsion and/or steric hindrance, and help regulate the transcription factor activity of the proteins [2, 1].
- Rederence
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- Insights into transcription enhancer factor 1 (TEF-1) activity from the solution structure of the TEA domain. Anbanandam A, Albarado DC, Nguyen CT, Halder G, Gao X, Veeraraghavan S. Proc. Natl. Acad. Sci. U.S.A. 103, 17225-30, (2006).
- An evolutionary, structural and functional overview of the mammalian TEAD1 and TEAD2 transcription factors. Landin-Malt A, Benhaddou A, Zider A, Flagiello D. Gene 591, 292-303, (2016).
- Characterization of the transcription activation function and the DNA binding domain of transcriptional enhancer factor-1. Hwang JJ, Chambon P, Davidson I. EMBO J. 12, 2337-48, (1993).
