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1ci4
From Proteopedia
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| - | [[Image:1ci4.gif|left|200px]] | + | [[Image:1ci4.gif|left|200px]] |
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| - | '''THE CRYSTAL STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR (BAF)''' | + | {{Structure |
| + | |PDB= 1ci4 |SIZE=350|CAPTION= <scene name='initialview01'>1ci4</scene>, resolution 1.90Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''THE CRYSTAL STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR (BAF)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CI4 is a [ | + | 1CI4 is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10924106 10924106] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: retroviral integration]] | [[Category: retroviral integration]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:24:37 2008'' |
Revision as of 08:24, 20 March 2008
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| , resolution 1.90Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mar 20 10:24:37 2008
