1svc
From Proteopedia
(New page: 200px<br /> <applet load="1svc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1svc, resolution 2.600Å" /> '''NFKB P50 HOMODIMER...) |
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| - | [[Image:1svc.gif|left|200px]]<br /> | + | [[Image:1svc.gif|left|200px]]<br /><applet load="1svc" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1svc" size=" | + | |
caption="1svc, resolution 2.600Å" /> | caption="1svc, resolution 2.600Å" /> | ||
'''NFKB P50 HOMODIMER BOUND TO DNA'''<br /> | '''NFKB P50 HOMODIMER BOUND TO DNA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of a large fragment of the p50 subunit of the human | + | 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== | ==About this Structure== | ||
| - | 1SVC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1SVC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SVC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Harrison, S | + | [[Category: Harrison, S C.]] |
| - | [[Category: Mueller, C | + | [[Category: Mueller, C W.]] |
[[Category: activator]] | [[Category: activator]] | ||
[[Category: dna]] | [[Category: dna]] | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:05:33 2008'' |
Revision as of 13:05, 21 February 2008
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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 Thu Feb 21 15:05:33 2008
