2bzf

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(New page: 200px<br /> <applet load="2bzf" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bzf, resolution 2.87&Aring;" /> '''STRUCTURAL BASIS FO...)
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[[Image:2bzf.gif|left|200px]]<br />
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[[Image:2bzf.gif|left|200px]]<br /><applet load="2bzf" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="2bzf" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2bzf, resolution 2.87&Aring;" />
caption="2bzf, resolution 2.87&Aring;" />
'''STRUCTURAL BASIS FOR DNA BRIDGING BY BARRIER-TO-AUTOINTEGRATION FACTOR (BAF)'''<br />
'''STRUCTURAL BASIS FOR DNA BRIDGING BY BARRIER-TO-AUTOINTEGRATION FACTOR (BAF)'''<br />
==Overview==
==Overview==
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The ability of barrier-to-autointegration factor (BAF) to bind and bridge, DNA in a sequence-independent manner is crucial for its role in retroviral, integration and a variety of cellular processes. To better understand this, behavior, we solved the crystal structure of BAF bound to DNA. The, structure reveals that BAF bridges DNA using two pairs of, helix-hairpin-helix motifs located on opposite surfaces of the BAF dimer, without changing its conformation.
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The ability of barrier-to-autointegration factor (BAF) to bind and bridge DNA in a sequence-independent manner is crucial for its role in retroviral integration and a variety of cellular processes. To better understand this behavior, we solved the crystal structure of BAF bound to DNA. The structure reveals that BAF bridges DNA using two pairs of helix-hairpin-helix motifs located on opposite surfaces of the BAF dimer without changing its conformation.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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2BZF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BZF OCA].
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2BZF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=2BZF OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Bradley, C.M.]]
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[[Category: Bradley, C M.]]
[[Category: Craigie, R.]]
[[Category: Craigie, R.]]
[[Category: Dyda, F.]]
[[Category: Dyda, F.]]
[[Category: Ghirlando, R.]]
[[Category: Ghirlando, R.]]
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[[Category: Ronning, D.R.]]
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[[Category: Ronning, D R.]]
[[Category: dna compaction]]
[[Category: dna compaction]]
[[Category: lem family]]
[[Category: lem family]]
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[[Category: retroviral integration]]
[[Category: retroviral integration]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:08:27 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:43:17 2008''

Revision as of 14:43, 21 February 2008


2bzf, resolution 2.87Å

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STRUCTURAL BASIS FOR DNA BRIDGING BY BARRIER-TO-AUTOINTEGRATION FACTOR (BAF)

Contents

Overview

The ability of barrier-to-autointegration factor (BAF) to bind and bridge DNA in a sequence-independent manner is crucial for its role in retroviral integration and a variety of cellular processes. To better understand this behavior, we solved the crystal structure of BAF bound to DNA. The structure reveals that BAF bridges DNA using two pairs of helix-hairpin-helix motifs located on opposite surfaces of the BAF dimer without changing its conformation.

Disease

Known disease associated with this structure: Epilepsy, myoclonic, benign adult familial OMIM:[601068]

About this Structure

2BZF is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis for DNA bridging by barrier-to-autointegration factor., Bradley CM, Ronning DR, Ghirlando R, Craigie R, Dyda F, Nat Struct Mol Biol. 2005 Oct;12(10):935-6. Epub 2005 Sep 11. PMID:16155580

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