1lei
From Proteopedia
(New page: 200px<br /> <applet load="1lei" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lei, resolution 2.7Å" /> '''The kB DNA sequence ...) |
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| - | [[Image:1lei.gif|left|200px]]<br /> | + | [[Image:1lei.gif|left|200px]]<br /><applet load="1lei" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1lei" size=" | + | |
caption="1lei, resolution 2.7Å" /> | caption="1lei, resolution 2.7Å" /> | ||
'''The kB DNA sequence from the HLV-LTR functions as an allosteric regulator of HIV transcription'''<br /> | '''The kB DNA sequence from the HLV-LTR functions as an allosteric regulator of HIV transcription'''<br /> | ||
==Overview== | ==Overview== | ||
| - | NF-kappaB is an inducible transcription factor involved in the immune | + | NF-kappaB is an inducible transcription factor involved in the immune response, inflammation, and viral transcription. To address how the two NF-kappaB and three Sp1 binding sites of the human immunodeficiency virus (HIV) long terminal repeat (LTR) control multiple activator assembly and transcription, we first observed and compared unique conformations between the crystallographic structure of the NF-kappaB p50.p65 heterodimer bound to the uPA-kappaB target site to that of the p50.p65.HIV-kappaB complex. Next, cooperativity between two NF-kappaB molecules bound to tandem HIV-kappaB sequences was measured as well as that of NF-kappaB and transcription factor Sp1 when bound to adjacent sites. The cooperativity of hybrid HIV-LTR enhancers was measured with the 3' kappaB site converted to uPA-kappaB or to interferon beta gene enhancer kappaB. The hybrids were defective in transcriptional activator assembly and less active transcriptionally. These functional differences correlate with observed conformational differences and demonstrate that distinct kappaB DNA sequences function as allosteric regulators in a gene-specific manner. |
==About this Structure== | ==About this Structure== | ||
| - | 1LEI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1LEI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1LEI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Chen-Park, F.]] | [[Category: Chen-Park, F.]] | ||
[[Category: Ghosh, G.]] | [[Category: Ghosh, G.]] | ||
| - | [[Category: Huang, D | + | [[Category: Huang, D B.]] |
[[Category: crystal structure]] | [[Category: crystal structure]] | ||
[[Category: nf-kb/dna complex]] | [[Category: nf-kb/dna complex]] | ||
[[Category: transcription factor]] | [[Category: transcription factor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:44:18 2008'' |
Revision as of 11:44, 21 February 2008
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The kB DNA sequence from the HLV-LTR functions as an allosteric regulator of HIV transcription
Overview
NF-kappaB is an inducible transcription factor involved in the immune response, inflammation, and viral transcription. To address how the two NF-kappaB and three Sp1 binding sites of the human immunodeficiency virus (HIV) long terminal repeat (LTR) control multiple activator assembly and transcription, we first observed and compared unique conformations between the crystallographic structure of the NF-kappaB p50.p65 heterodimer bound to the uPA-kappaB target site to that of the p50.p65.HIV-kappaB complex. Next, cooperativity between two NF-kappaB molecules bound to tandem HIV-kappaB sequences was measured as well as that of NF-kappaB and transcription factor Sp1 when bound to adjacent sites. The cooperativity of hybrid HIV-LTR enhancers was measured with the 3' kappaB site converted to uPA-kappaB or to interferon beta gene enhancer kappaB. The hybrids were defective in transcriptional activator assembly and less active transcriptionally. These functional differences correlate with observed conformational differences and demonstrate that distinct kappaB DNA sequences function as allosteric regulators in a gene-specific manner.
About this Structure
1LEI is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
The kappa B DNA sequence from the HIV long terminal repeat functions as an allosteric regulator of HIV transcription., Chen-Park FE, Huang DB, Noro B, Thanos D, Ghosh G, J Biol Chem. 2002 Jul 5;277(27):24701-8. Epub 2002 Apr 22. PMID:11970949
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