Structure of NF-κB p50 homodimer bound to a κB site
NaturePublished 1 January 1995
Gourisankar Ghosh, Gregory Van Duyne, Sankar Ghosh, Paul B. Sigler
Citations568
SJR quartileQ1
SJR score18.29
SNIP10.16
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Abstract
The 2.3-Â crystal structure of the transcription factor NF-κB p50 homodimer bound to a palindromic κB 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 κB recognition site mainly through loops connecting secondary structure elements in both domains. The carboxy-terminal domains form a dimerization interface between β-sheets using residues that are strongly conserved in the Rel family.
Keywords
Immunology and MicrobiologyBiochemistry, Genetics and Molecular Biology
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