Abstract
The 2.3-A crystal structure of the transcription factor NK-kappa B p50 homodimer bound to a palindromic kappa B site reveals that the Rel homology region folds into two distinct domains, similar to those in the immunoglobulin superfamily. The p50 dimer envelopes an undistorted B-DNA helix, making specific contacts along the 10-base-pair kappa B recognition site mainly through loops connecting secondary structure elements in both domains. The carboxy-terminal domains form a dimerization interface between beta-sheets using residues that are strongly conserved in the Rel family.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Computer Graphics
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Crystallography, X-Ray
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DNA / chemistry*
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Drosophila
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Humans
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Immunoglobulins / chemistry
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Mice
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Molecular Sequence Data
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NF-kappa B / chemistry*
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NF-kappa B / metabolism
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NF-kappa B p50 Subunit
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Nucleic Acid Conformation
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Protein Binding
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Protein Conformation
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Proto-Oncogene Proteins / metabolism
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Proto-Oncogene Proteins c-rel
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RNA
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Sequence Homology, Amino Acid
Substances
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Immunoglobulins
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NF-kappa B
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NF-kappa B p50 Subunit
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Proto-Oncogene Proteins
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Proto-Oncogene Proteins c-rel
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RNA
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DNA