Nature Structural Biology
3, 224 - 227 (1996)
doi:10.1038/nsb0396-224
Comparison of two different DMA-binding modes of the NF- B p50 homodimerChristoph W. Müller1, 2, Félix A. Rey1, 3
& Stephen C. Harrison1
1Howard Hughes Medical Institute and Harvard University Department of Molecular and Cellular Biology, 7 Divinity Avenue, Cambridge, Massachusetts 02138, USA
2Present Address: EMBL, Grenoble Outstation, c/o lLL BP156, F-38042 Grenoble CEDEX 9, France
3Present Address: Laboratoire de Biologie Structural, CNRS - Bat. 34,1, Ave. de la Terrasse 91198 Gif-sur-Yvette Cedex France Analysis of the NF- B p50 homodimer bound to different DNA sequences shows that the protein can recognize half-site spacings of either three or four base pairs. The protein can maintain most of its DNA contacts by a relative reorientation of its two domains.
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