1ci4: Difference between revisions

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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"

<applet load="1ci4" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1ci4, resolution 1.90Å" />

'''THE CRYSTAL STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR (BAF)'''<br />

==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.

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==

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==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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1CI4 OCA].

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==

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[[Category: Single protein]]

[[Category: Craigie, R.]]

[[Category: Davies, D.R.]]

[[Category: Davies, D R.]]

[[Category: Umland, T.C.]]

[[Category: Umland, T C.]]

[[Category: Wei, S.Q.]]

[[Category: Wei, S Q.]]

[[Category: dna binding protein]]

[[Category: preintegration complex]]

[[Category: retroviral integration]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov~~ 12 16:21:~~51 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:06:18 2008''

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@@ Line 1: / Line 1: @@
-[[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"
-<applet load="1ci4" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1ci4, resolution 1.90&Aring;" />
 '''THE CRYSTAL STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR (BAF)'''<br />
 ==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.
+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==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-CI4 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CI4 OCA].
+CI4 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==
@@ Line 18: / Line 17: @@
 [[Category: Single protein]]
 [[Category: Craigie, R.]]
-[[Category: Davies, D.R.]]
+[[Category: Davies, D R.]]
-[[Category: Umland, T.C.]]
+[[Category: Umland, T C.]]
-[[Category: Wei, S.Q.]]
+[[Category: Wei, S Q.]]
 [[Category: dna binding protein]]
 [[Category: preintegration complex]]
 [[Category: retroviral integration]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:21:51 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:06:18 2008''