Nature. 1995 Jan 26;373(6512):311-7.

Structure of the NF-kappa B p50 homodimer bound to DNA.

Müller CW, Rey FA, Sodeoka M, Verdine GL, Harrison SC.

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Howard Hughes Medical Institute, Cambridge, Massachusetts 02138.

Abstract

The structure of a large fragment of the p50 subunit of the human transcription factor NF-kappa B, bound as a homodimer to DNA, reveals that the Rel-homology region has two beta-barrel domains that grip DNA in the major groove. Both domains contact the DNA backbone. The amino-terminal specificity domain contains a recognition loop that interacts with DNA bases; the carboxy-terminal dimerization domain bears the site of I-kappa B interaction. The folds of these domains are related to immunoglobulin-like modules. The amino-terminal domain also resembles the core domain of p53.

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DNA-binding proteins. A butterfly flutters by. [Nature. 1995]
DNA-binding proteins. A butterfly flutters by.Baltimore D, Beg AA. Nature. 1995 Jan 26; 373(6512):287-8.

PMID:: 7830764; [PubMed - indexed for MEDLINE]

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Structures reported by this article

Nfkb P50 Homodimer Bound To Dna

PDB: 1SVC

Source: Homo sapiens, synthetic construct

Method: X-Ray Diffraction

Resolution: 2.6 Å

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