1z1d

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[[Image:1z1d.gif|left|200px]]
 
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==Structural Model for the interaction between RPA32 C-terminal domain and SV40 T antigen origin binding domain.==
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The line below this paragraph, containing "STRUCTURE_1z1d", creates the "Structure Box" on the page.
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<StructureSection load='1z1d' size='340' side='right'caption='[[1z1d]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1z1d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Macaca_mulatta_polyomavirus_1 Macaca mulatta polyomavirus 1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z1D FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1z1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z1d OCA], [https://pdbe.org/1z1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z1d RCSB], [https://www.ebi.ac.uk/pdbsum/1z1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z1d ProSAT]</span></td></tr>
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{{STRUCTURE_1z1d| PDB=1z1d | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RFA2_HUMAN RFA2_HUMAN] Required for DNA recombination, repair and replication. The activity of RP-A is mediated by single-stranded DNA binding and protein interactions. Required for the efficient recruitment of the DNA double-strand break repair factor RAD51 to chromatin in response to DNA damage.<ref>PMID:15205463</ref> <ref>PMID:19116208</ref> <ref>PMID:19996105</ref> <ref>PMID:20154705</ref> Functions as component of the alternative replication protein A complex (aRPA). aRPA binds single-stranded DNA and probably plays a role in DNA repair; it does not support chromosomal DNA replication and cell cycle progression through S-phase. In vitro, aRPA cannot promote efficient priming by DNA polymerase alpha but supports DNA polymerase delta synthesis in the presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange.<ref>PMID:15205463</ref> <ref>PMID:19116208</ref> <ref>PMID:19996105</ref> <ref>PMID:20154705</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z1/1z1d_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1z1d ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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'''Structural Model for the interaction between RPA32 C-terminal domain and SV40 T antigen origin binding domain.'''
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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<ref>PMID:15793585</ref>
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==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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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1Z1D is a [[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].
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</div>
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<div class="pdbe-citations 1z1d" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15793585 15793585]
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*[[Large T Antigen|Large T Antigen]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Simian virus 40]]
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[[Category: Macaca mulatta polyomavirus 1]]
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[[Category: Arunkumar, A I.]]
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[[Category: Arunkumar AI]]
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[[Category: Chazin, W J.]]
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[[Category: Chazin WJ]]
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[[Category: Fanning, E.]]
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[[Category: Fanning E]]
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[[Category: Jiang, X.]]
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[[Category: Jiang X]]
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[[Category: Klimovich, V.]]
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[[Category: Klimovich V]]
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[[Category: Mizoue, L.]]
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[[Category: Mizoue L]]
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[[Category: Ott, R D.]]
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[[Category: Ott RD]]
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[[Category: Origin binding domain]]
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[[Category: Protein-protein complex]]
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[[Category: Winged helix-turn-helix motif]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:04:13 2008''
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Current revision

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

PDB ID 1z1d

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