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XB-ART-8694
Cell 2001 Jul 13;1061:71-81. doi: 10.1016/s0092-8674(01)00417-2.
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Crystal structure of negative cofactor 2 recognizing the TBP-DNA transcription complex.

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


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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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Species referenced: Xenopus laevis
Genes referenced: dr1 h2ac21 h2bc21 tbp