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245	1	0	_aCrystal Structure of Negative Cofactor 2 Recognizing the TBP-DNA Transcription Complex
490	0		_vCell, 106(1), p.71-81, 2001
520	3		_aThe 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 a and ß 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. NC2ß contributes to inhibition of TATA-dependent transcription through interactions of its C-terminal a helix with a conserved hydrophobic feature on the upper surface of TBP, which in turn positions the penultimate a helix of NC2ß to block recognition of the TBP-DNA complex by transcription factor IIB. Further regulatory implications of the NC2 heterodimer structure are discussed.
700	1	2	_aKamada, K.
700	1	2	_aShu, F.
700	1	2	_aChen, H.
700	1	2	_aMalik, S.
700	1	2	_aStelzer, G.
700	1	2	_aRoeder, R.G.
700	1	2	_aMeisterernst, M.
700	1	2	_aMeisterernst, M.
856	4	0	_uhttps://drive.google.com/file/d/18TkaTCYHbGexUAQhKdYuwmUwR8GwdbvA/view?usp=drivesdk _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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