Solution structure of the C-terminal core domain of human TFIIB: similarity to cyclin A and interaction with TATA-binding protein.
TFIIB is an essential component of the machinery that transcribes protein-coding genes. The three-dimensional structure of the human TFIIB core domain (TFIIBc) has been determined using multidimensional heteronuclear magnetic resonance spectroscopy. The molecule consists of two direct repeats that adopt similar alpha-helical folds, conferring pseudo-twofold symmetry. An extensive, central basic ... surface including an amphipathic alpha helix is critical to the function of TFIIB as a bridge between the TBP-promoter complex and RNA polymerase II and associated general and regulatory transcription factors. Similarities between the TFIIBc and cyclin A folds indicate that elements of the eukaryotic cell cycle control apparatus evolved from more fundamental transcriptional control components, demonstrating a link between the transcription and cell cycle molecular machineries.
Mesh Terms:
Amino Acid Sequence, Binding Sites, Cyclins, DNA, DNA-Binding Proteins, Humans, Image Processing, Computer-Assisted, Magnetic Resonance Spectroscopy, Molecular Sequence Data, Promoter Regions, Genetic, Protein Conformation, Sequence Homology, Amino Acid, TATA Box, TATA-Box Binding Protein, Transcription Factor TFIIB, Transcription Factors, Transcription, Genetic
Amino Acid Sequence, Binding Sites, Cyclins, DNA, DNA-Binding Proteins, Humans, Image Processing, Computer-Assisted, Magnetic Resonance Spectroscopy, Molecular Sequence Data, Promoter Regions, Genetic, Protein Conformation, Sequence Homology, Amino Acid, TATA Box, TATA-Box Binding Protein, Transcription Factor TFIIB, Transcription Factors, Transcription, Genetic
Cell
Date: Sep. 08, 1995
PubMed ID: 7671313
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