1ci4
From Proteopedia
(New page: 200px<br /> <applet load="1ci4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ci4, resolution 1.90Å" /> '''THE CRYSTAL STRUCTU...) |
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| - | [[Image:1ci4.gif|left|200px]]<br /> | + | [[Image:1ci4.gif|left|200px]]<br /><applet load="1ci4" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1ci4, resolution 1.90Å" /> | caption="1ci4, resolution 1.90Å" /> | ||
'''THE CRYSTAL STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR (BAF)'''<br /> | '''THE CRYSTAL STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR (BAF)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Barrier-to-autointegration factor (BAF) is a host cell protein that plays | + | Barrier-to-autointegration factor (BAF) is a host cell protein that plays a crucial role in retroviral integration. Preintegration complexes (PICs) stripped of BAF lose their normal integration activity, which can be restored by incubation with purified BAF. BAF bridges double-stranded DNA both intra- and intermolecularly in a non-sequence-specific manner, leading to the formation of a nucleoprotein network. BAF also binds to the nuclear protein lamina-associated polypeptide 2 (LAP2), and is localized with chromatin during interphase and mitosis. The crystal structure of homodimeric human BAF has been determined to 1.9 A resolution. The fold of the BAF monomer resembles that of the second domain of RuvA. This comparison revealed the presence of the helix-hairpin-helix (HhH) nonspecific DNA binding motif within BAF. A novel feature of BAF's HhH motif is the occupation of the metal binding site by the epsilon-amino group of Lys 6, providing an alternative means of sequestering positive charge. Mutational analysis corroborates the HhH motif's prominent role in DNA binding and argues against a previously proposed helix-turn-helix (HTH) binding site located in another region of the monomer. A model of BAF bridging DNA via the HhH motif is proposed. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CI4 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:// | + | 1CI4 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=1CI4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Craigie, R.]] | [[Category: Craigie, R.]] | ||
| - | [[Category: Davies, D | + | [[Category: Davies, D R.]] |
| - | [[Category: Umland, T | + | [[Category: Umland, T C.]] |
| - | [[Category: Wei, S | + | [[Category: Wei, S Q.]] |
[[Category: dna binding protein]] | [[Category: dna binding protein]] | ||
[[Category: preintegration complex]] | [[Category: preintegration complex]] | ||
[[Category: retroviral integration]] | [[Category: retroviral integration]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:06:18 2008'' |
Revision as of 10:06, 21 February 2008
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THE CRYSTAL STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR (BAF)
Contents |
Overview
Barrier-to-autointegration factor (BAF) is a host cell protein that plays a crucial role in retroviral integration. Preintegration complexes (PICs) stripped of BAF lose their normal integration activity, which can be restored by incubation with purified BAF. BAF bridges double-stranded DNA both intra- and intermolecularly in a non-sequence-specific manner, leading to the formation of a nucleoprotein network. BAF also binds to the nuclear protein lamina-associated polypeptide 2 (LAP2), and is localized with chromatin during interphase and mitosis. The crystal structure of homodimeric human BAF has been determined to 1.9 A resolution. The fold of the BAF monomer resembles that of the second domain of RuvA. This comparison revealed the presence of the helix-hairpin-helix (HhH) nonspecific DNA binding motif within BAF. A novel feature of BAF's HhH motif is the occupation of the metal binding site by the epsilon-amino group of Lys 6, providing an alternative means of sequestering positive charge. Mutational analysis corroborates the HhH motif's prominent role in DNA binding and argues against a previously proposed helix-turn-helix (HTH) binding site located in another region of the monomer. A model of BAF bridging DNA via the HhH motif is proposed.
Disease
Known disease associated with this structure: Epilepsy, myoclonic, benign adult familial OMIM:[601068]
About this Structure
1CI4 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis of DNA bridging by barrier-to-autointegration factor., Umland TC, Wei SQ, Craigie R, Davies DR, Biochemistry. 2000 Aug 8;39(31):9130-8. PMID:10924106
Page seeded by OCA on Thu Feb 21 12:06:18 2008
