NF‐κB p52:RelB heterodimer recognizes two classes of κB sites with two distinct modes
Copyright policy )NF‐κB p52:RelB heterodimer recognizes two classes of κB sites with two distinct modes
The X‐ray structure of the nuclear factor‐κB (NF‐κB) p52:RelB:κB DNA complex reveals a new recognition feature not previously seen in other NF‐κB:κB DNA complexes. Arg 125 of RelB is in contact with an additional DNA base pair. Surprisingly, the p52:RelB R125A mutant heterodimer shows defects both in DNA binding and in transcriptional activity only to a subclass of κB sites. We found that the Arg 125‐sensitive κB sites contain more contiguous and centrally located A:T base pairs than do the insensitive sites. A protein‐induced kink observed in this complex, which used an AT‐rich κB site, might allow the DNA contact by Arg 125; such a kink might not be possible in complexes with non‐AT‐rich κB sites. Furthermore, we show that the p52:RelB heterodimer binds to a broader spectrum of κB sites when compared with the p50:RelA heterodimer. We suggest that the p52:RelB heterodimer is more adaptable to complement sequence and structural variations in κB sites when compared with other NF‐κB dimers.
- University of California, San Diego United States
- University of California, San Diego United States
Models, Molecular, Base Composition, Molecular Sequence Data, Transcription Factor RelB, DNA, Crystallography, X-Ray, Protein Structure, Tertiary, Substrate Specificity, Mice, Structure-Activity Relationship, Amino Acid Substitution, NF-kappa B p52 Subunit, Protein Interaction Mapping, Animals, Humans, Point Mutation, Amino Acid Sequence, Dimerization, Sequence Alignment, Protein Binding
Models, Molecular, Base Composition, Molecular Sequence Data, Transcription Factor RelB, DNA, Crystallography, X-Ray, Protein Structure, Tertiary, Substrate Specificity, Mice, Structure-Activity Relationship, Amino Acid Substitution, NF-kappa B p52 Subunit, Protein Interaction Mapping, Animals, Humans, Point Mutation, Amino Acid Sequence, Dimerization, Sequence Alignment, Protein Binding
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