| Title |
Solution structure of the c-terminal core domain of human TFIIB: Similarity to cyclin A and interaction with TATA-binding protein
|
|---|---|
| Published in |
Cell, September 1995
|
| DOI | 10.1016/0092-8674(95)90483-2 |
| Pubmed ID | |
| Authors | |
| Abstract |
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. |
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Mendeley demographics
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| United Kingdom | 1 | 2% |
| Unknown | 44 | 98% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Ph. D. Student | 16 | 36% |
| Researcher | 6 | 13% |
| Professor > Associate Professor | 5 | 11% |
| Student > Master | 4 | 9% |
| Professor | 3 | 7% |
| Other | 6 | 13% |
| Unknown | 5 | 11% |
| Readers by discipline | Count | As % |
|---|---|---|
| Agricultural and Biological Sciences | 18 | 40% |
| Biochemistry, Genetics and Molecular Biology | 9 | 20% |
| Chemistry | 4 | 9% |
| Immunology and Microbiology | 2 | 4% |
| Arts and Humanities | 1 | 2% |
| Other | 3 | 7% |
| Unknown | 8 | 18% |