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1nfk

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(New page: 200px<br /><applet load="1nfk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nfk, resolution 2.300&Aring;" /> '''STRUCTURE OF THE NU...)
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[[Image:1nfk.jpg|left|200px]]<br /><applet load="1nfk" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1nfk.jpg|left|200px]]<br /><applet load="1nfk" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1nfk, resolution 2.300&Aring;" />
caption="1nfk, resolution 2.300&Aring;" />
'''STRUCTURE OF THE NUCLEAR FACTOR KAPPA-B (NF-KB) P50 HOMODIMER'''<br />
'''STRUCTURE OF THE NUCLEAR FACTOR KAPPA-B (NF-KB) P50 HOMODIMER'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1NFK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NFK OCA].
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1NFK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NFK OCA].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Duyne, G.Van.]]
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[[Category: Duyne, G Van.]]
[[Category: Ghosh, G.]]
[[Category: Ghosh, G.]]
[[Category: Ghosh, S.]]
[[Category: Ghosh, S.]]
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[[Category: Sigler, P.B.]]
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[[Category: Sigler, P B.]]
[[Category: complex (transcription factor/dna)]]
[[Category: complex (transcription factor/dna)]]
[[Category: nf-kb p50]]
[[Category: nf-kb p50]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:12:57 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:05:34 2008''

Revision as of 12:05, 21 February 2008


1nfk, resolution 2.300Å

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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

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