1z1d

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(New page: 200px<br /> <applet load="1z1d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z1d" /> '''Structural Model for the interaction betwee...)
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<applet load="1z1d" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Structural Model for the interaction between RPA32 C-terminal domain and SV40 T antigen origin binding domain.'''<br />
'''Structural Model for the interaction between RPA32 C-terminal domain and SV40 T antigen origin binding domain.'''<br />
==Overview==
==Overview==
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Simian virus 40 (SV40) provides a model system for the study of eukaryotic, DNA replication, in which the viral protein, large T antigen (Tag), marshals human proteins to replicate the viral minichromosome. SV40, replication requires interaction of Tag with the host single-stranded, DNA-binding protein, replication protein A (hRPA). The C-terminal domain, of the hRPA32 subunit (RPA32C) facilitates initiation of replication, but, whether it interacts with Tag is not known. Affinity chromatography and, NMR revealed physical interaction between hRPA32C and the Tag origin, DNA-binding domain, and a structural model of the complex was determined., Point mutations were then designed to reverse charges in the binding, sites, resulting in substantially reduced binding affinity. Corresponding, mutations introduced into intact hRPA impaired initiation of replication, and primosome activity, implying that this interaction has a critical role, in assembly and progression of the SV40 replisome.
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Simian virus 40 (SV40) provides a model system for the study of eukaryotic DNA replication, in which the viral protein, large T antigen (Tag), marshals human proteins to replicate the viral minichromosome. SV40 replication requires interaction of Tag with the host single-stranded DNA-binding protein, replication protein A (hRPA). The C-terminal domain of the hRPA32 subunit (RPA32C) facilitates initiation of replication, but whether it interacts with Tag is not known. Affinity chromatography and NMR revealed physical interaction between hRPA32C and the Tag origin DNA-binding domain, and a structural model of the complex was determined. Point mutations were then designed to reverse charges in the binding sites, resulting in substantially reduced binding affinity. Corresponding mutations introduced into intact hRPA impaired initiation of replication and primosome activity, implying that this interaction has a critical role in assembly and progression of the SV40 replisome.
==About this Structure==
==About this Structure==
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1Z1D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Simian_virus_40 Simian virus 40]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Z1D OCA].
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1Z1D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Simian_virus_40 Simian virus 40]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z1D OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Simian virus 40]]
[[Category: Simian virus 40]]
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[[Category: Arunkumar, A.I.]]
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[[Category: Arunkumar, A I.]]
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[[Category: Chazin, W.J.]]
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[[Category: Chazin, W J.]]
[[Category: Fanning, E.]]
[[Category: Fanning, E.]]
[[Category: Jiang, X.]]
[[Category: Jiang, X.]]
[[Category: Klimovich, V.]]
[[Category: Klimovich, V.]]
[[Category: Mizoue, L.]]
[[Category: Mizoue, L.]]
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[[Category: Ott, R.D.]]
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[[Category: Ott, R D.]]
[[Category: origin binding domain]]
[[Category: origin binding domain]]
[[Category: protein-protein complex]]
[[Category: protein-protein complex]]
[[Category: winged helix-turn-helix motif]]
[[Category: winged helix-turn-helix motif]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:28:18 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:11:11 2008''

Revision as of 14:11, 21 February 2008


1z1d

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Structural Model for the interaction between RPA32 C-terminal domain and SV40 T antigen origin binding domain.

Overview

Simian virus 40 (SV40) provides a model system for the study of eukaryotic DNA replication, in which the viral protein, large T antigen (Tag), marshals human proteins to replicate the viral minichromosome. SV40 replication requires interaction of Tag with the host single-stranded DNA-binding protein, replication protein A (hRPA). The C-terminal domain of the hRPA32 subunit (RPA32C) facilitates initiation of replication, but whether it interacts with Tag is not known. Affinity chromatography and NMR revealed physical interaction between hRPA32C and the Tag origin DNA-binding domain, and a structural model of the complex was determined. Point mutations were then designed to reverse charges in the binding sites, resulting in substantially reduced binding affinity. Corresponding mutations introduced into intact hRPA impaired initiation of replication and primosome activity, implying that this interaction has a critical role in assembly and progression of the SV40 replisome.

About this Structure

1Z1D is a Protein complex structure of sequences from Homo sapiens and Simian virus 40. Full crystallographic information is available from OCA.

Reference

Insights into hRPA32 C-terminal domain--mediated assembly of the simian virus 40 replisome., Arunkumar AI, Klimovich V, Jiang X, Ott RD, Mizoue L, Fanning E, Chazin WJ, Nat Struct Mol Biol. 2005 Apr;12(4):332-9. Epub 2005 Mar 27. PMID:15793585

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