Article
Structural and functional analysis of mutations along the crystallographic dimer interface of the yeast TATA binding protein.
Molecular and cellular biology - 1 May 2003
Kou Haiping, Irvin Jordan D, Huisinga Kathryn L, Mitra Madhusmita, Pugh B Franklin
Abstract excerpt
The TATA binding protein (TBP) is a central component of the eukaryotic transcription machinery and is subjected to both positive and negative regulation. As is evident from structural and functional studies, TBP's concave DNA binding surface is inhibited by a number of potential mechanisms, including homodimerization and binding to the TAND domain of the TFIID subunit TAF1 (yTAF(II)145/130). Here we further...
Topics
- Adenosine Triphosphatases
- Binding Sites
- Cell Division
- Crystallography, X-Ray
- DNA Helicases
- Dimerization
- Gene Expression Regulation, Fungal
- Models, Molecular
- Mutagenesis, Site-Directed
- Mutation
- Phenotype
- Protein Conformation
- Protein Structure, Tertiary