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Crystal structure of negative cofactor 2 recognizing the TBP-DNA transcription complex.

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.

Pubmed ID: 11461703

Authors

  • Kamada K
  • Shu F
  • Chen H
  • Malik S
  • Stelzer G
  • Roeder RG
  • Meisterernst M
  • Burley SK

Journal

Cell

Publication Data

July 13, 2001

Associated Grants

None

Mesh Terms

  • Amino Acid Sequence
  • Animals
  • Caenorhabditis elegans
  • Crystallography, X-Ray
  • DNA
  • DNA-Binding Proteins
  • Drosophila melanogaster
  • Histones
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Phosphoproteins
  • Protein Structure, Secondary
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Static Electricity
  • TATA Box
  • TATA-Box Binding Protein
  • Transcription Factor TFIIA
  • Transcription Factor TFIIB
  • Transcription Factors
  • Transcription, Genetic
  • Xenopus laevis