1nfk

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[[Image:1nfk.jpg|left|200px]]
[[Image:1nfk.jpg|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nfk OCA], [http://www.ebi.ac.uk/pdbsum/1nfk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nfk RCSB]</span>
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'''STRUCTURE OF THE NUCLEAR FACTOR KAPPA-B (NF-KB) P50 HOMODIMER'''
'''STRUCTURE OF THE NUCLEAR FACTOR KAPPA-B (NF-KB) P50 HOMODIMER'''
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[[Category: Ghosh, S.]]
[[Category: Ghosh, S.]]
[[Category: Sigler, P B.]]
[[Category: Sigler, P B.]]
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[[Category: complex (transcription factor/dna)]]
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[[Category: Nf-kb p50]]
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[[Category: nf-kb p50]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:28:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:29:40 2008''
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Revision as of 23:28, 2 May 2008

Image:1nfk.jpg

Template:STRUCTURE 1nfk

STRUCTURE OF THE NUCLEAR FACTOR KAPPA-B (NF-KB) P50 HOMODIMER


Overview

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.

About this Structure

1NFK is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Structure of NF-kappa B p50 homodimer bound to a kappa B site., Ghosh G, van Duyne G, Ghosh S, Sigler PB, Nature. 1995 Jan 26;373(6512):303-10. PMID:7530332 Page seeded by OCA on Sat May 3 02:28:30 2008

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