1svc: Difference between revisions
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'''NFKB P50 HOMODIMER BOUND TO DNA''' | '''NFKB P50 HOMODIMER BOUND TO DNA''' | ||
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[[Category: Harrison, S C.]] | [[Category: Harrison, S C.]] | ||
[[Category: Mueller, C W.]] | [[Category: Mueller, C W.]] | ||
[[Category: | [[Category: Activator]] | ||
[[Category: | [[Category: Dna]] | ||
[[Category: | [[Category: Dna-binding]] | ||
[[Category: | [[Category: Nuclear protein]] | ||
[[Category: | [[Category: Phosphorylation]] | ||
[[Category: | [[Category: Repeat]] | ||
[[Category: | [[Category: Transcription regulation]] | ||
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Revision as of 06:10, 3 May 2008
NFKB P50 HOMODIMER BOUND TO DNA
Overview
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.
About this Structure
1SVC is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the NF-kappa B p50 homodimer bound to DNA., Muller CW, Rey FA, Sodeoka M, Verdine GL, Harrison SC, Nature. 1995 Jan 26;373(6512):311-7. PMID:7830764 Page seeded by OCA on Sat May 3 09:10:33 2008