| Title |
Crystal Structure of Negative Cofactor 2 Recognizing the TBP-DNA Transcription Complex
|
|---|---|
| Published in |
Cell, July 2001
|
| DOI | 10.1016/s0092-8674(01)00417-2 |
| Pubmed ID | |
| Authors | |
| Abstract |
The X-ray structure of a ternary complex of Negative Cofactor 2 (NC2), the TATA box binding protein (TBP), and DNA has been determined at 2.6 A resolution. The N termini of NC2 alpha and beta resemble histones H2A and H2B, respectively, and form a heterodimer that binds to the bent DNA double helix on the underside of the preformed TBP-DNA complex via electrostatic interactions. NC2beta contributes to inhibition of TATA-dependent transcription through interactions of its C-terminal alpha helix with a conserved hydrophobic feature on the upper surface of TBP, which in turn positions the penultimate alpha helix of NC2beta to block recognition of the TBP-DNA complex by transcription factor IIB. Further regulatory implications of the NC2 heterodimer structure are discussed. |
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Mendeley demographics
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Russia | 1 | 1% |
| Germany | 1 | 1% |
| Czechia | 1 | 1% |
| Brazil | 1 | 1% |
| Unknown | 64 | 94% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Researcher | 14 | 21% |
| Student > Ph. D. Student | 12 | 18% |
| Professor > Associate Professor | 10 | 15% |
| Student > Master | 7 | 10% |
| Professor | 5 | 7% |
| Other | 11 | 16% |
| Unknown | 9 | 13% |
| Readers by discipline | Count | As % |
|---|---|---|
| Agricultural and Biological Sciences | 34 | 50% |
| Biochemistry, Genetics and Molecular Biology | 13 | 19% |
| Chemistry | 5 | 7% |
| Immunology and Microbiology | 2 | 3% |
| Arts and Humanities | 1 | 1% |
| Other | 3 | 4% |
| Unknown | 10 | 15% |