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pubmed-article:9383370pubmed:abstractTextMembers of the Rel family of transcription factors are important in regulating the inflammatory, acute phase, and immune responses in mammals. The structural basis for sequence-specific binding by Rel proteins is poorly understood, however. In the studies reported here, a new photoaffinity labeling procedure has been used to probe DNA contacts established by a Rel protein, the p50 homodimer of NF-kappa B.lld:pubmed
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pubmed-article:9383370pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:9383370pubmed:articleTitleDNA binding by an amino acid residue in the C-terminal half of the Rel homology region.lld:pubmed
pubmed-article:9383370pubmed:affiliationDepartment of Chemistry, Harvard University, Cambridge, MA 02138, USA.lld:pubmed
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