1ci4

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[[Image:1ci4.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ci4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ci4 OCA], [http://www.ebi.ac.uk/pdbsum/1ci4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ci4 RCSB]</span>
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'''THE CRYSTAL STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR (BAF)'''
'''THE CRYSTAL STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR (BAF)'''
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[[Category: Umland, T C.]]
[[Category: Umland, T C.]]
[[Category: Wei, S Q.]]
[[Category: Wei, S Q.]]
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[[Category: dna binding protein]]
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[[Category: Dna binding protein]]
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[[Category: preintegration complex]]
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[[Category: Preintegration complex]]
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[[Category: retroviral integration]]
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[[Category: Retroviral integration]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:45:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:22:12 2008''
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Revision as of 09:45, 2 May 2008

Template:STRUCTURE 1ci4

THE CRYSTAL STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR (BAF)


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.

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 Fri May 2 12:45:07 2008

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