1SVC

NFKB P50 HOMODIMER BOUND TO DNA

Summary for 1SVC

• Entry DOI: 10.2210/pdb1svc/pdb
• Descriptor: DNA (5'-D(*AP*GP*AP*TP*GP*GP*GP*GP*AP*AP*TP*CP*CP*CP*CP*TP*A P*GP*A)-3'), PROTEIN (NUCLEAR FACTOR KAPPA-B (NF-KB)) (3 entities in total)
• Functional Keywords: dna-binding, transcription regulation, activator, nuclear protein, phosphorylation, dna, transcription-dna complex, transcription/dna
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: P19838
• Total number of polymer chains: 2
• Total formula weight: 47007.68

Authors

Mueller, C.W.,Harrison, S.C. (deposition date: 1995-11-27, release date: 1996-06-10, Last modification date: 2024-02-14)

Primary citation

Muller, C.W.,Rey, F.A.,Sodeoka, M.,Verdine, G.L.,Harrison, S.C.
Structure of the NF-kappa B p50 homodimer bound to DNA.
Nature, 373:311-317, 1995

PubMed 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.

PubMed: 7830764
DOI: 10.1038/373311a0

Experimental method

X-RAY DIFFRACTION (2.6 Å)