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==HADDOCK calculated model of the complex between the BRCT region of RFC p140 and dsDNA==
==HADDOCK calculated model of the complex between the BRCT region of RFC p140 and dsDNA==
<StructureSection load='2k7f' size='340' side='right'caption='[[2k7f]], [[NMR_Ensembles_of_Models | 4 NMR models]]' scene=''>
<StructureSection load='2k7f' size='340' side='right'caption='[[2k7f]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2k7f]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K7F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K7F FirstGlance]. <br>
<table><tr><td colspan='2'>[[2k7f]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K7F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K7F FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2k6g|2k6g]], [[2ebu|2ebu]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RFC1, RFC140 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2k7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k7f OCA], [https://pdbe.org/2k7f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k7f RCSB], [https://www.ebi.ac.uk/pdbsum/2k7f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k7f ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2k7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k7f OCA], [https://pdbe.org/2k7f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k7f RCSB], [https://www.ebi.ac.uk/pdbsum/2k7f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k7f ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/RFC1_HUMAN RFC1_HUMAN]] The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. This subunit binds to the primer-template junction. Binds the PO-B transcription element as well as other GA rich DNA sequences. Could play a role in DNA transcription regulation as well as DNA replication and/or repair. Can bind single- or double-stranded DNA.<ref>PMID:8999859</ref>  Interacts with C-terminus of PCNA. 5' phosphate residue is required for binding of the N-terminal DNA-binding domain to duplex DNA, suggesting a role in recognition of non-primer template DNA structures during replication and/or repair.<ref>PMID:8999859</ref>
[https://www.uniprot.org/uniprot/RFC1_HUMAN RFC1_HUMAN] The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. This subunit binds to the primer-template junction. Binds the PO-B transcription element as well as other GA rich DNA sequences. Could play a role in DNA transcription regulation as well as DNA replication and/or repair. Can bind single- or double-stranded DNA.<ref>PMID:8999859</ref>  Interacts with C-terminus of PCNA. 5' phosphate residue is required for binding of the N-terminal DNA-binding domain to duplex DNA, suggesting a role in recognition of non-primer template DNA structures during replication and/or repair.<ref>PMID:8999859</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=2k7f ConSurf].
</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=2k7f ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BRCA1 C-terminal domain (BRCT)-containing proteins are found widely throughout the animal and bacteria kingdoms where they are exclusively involved in cell cycle regulation and DNA metabolism. Whereas most BRCT domains are involved in protein-protein interactions, a small subset has bona fide DNA binding activity. Here, we present the solution structure of the BRCT region of the large subunit of replication factor C bound to DNA and a model of the structure-specific complex with 5'-phosphorylated double-stranded DNA. The replication factor C BRCT domain possesses a large basic patch on one face, which includes residues that are structurally conserved and ligate the phosphate in phosphopeptide binding BRCT domains. An extra alpha-helix at the N terminus, which is required for DNA binding, inserts into the major groove and makes extensive contacts to the DNA backbone. The model of the protein-DNA complex suggests 5'-phosphate recognition by the BRCT domains of bacterial NAD(+)-dependent ligases and a nonclamp loading role for the replication factor C complex in DNA transactions.
Structure of the DNA-bound BRCA1 C-terminal region from human replication factor C p140 and model of the protein-DNA complex.,Kobayashi M, Ab E, Bonvin AM, Siegal G J Biol Chem. 2010 Mar 26;285(13):10087-97. Epub 2010 Jan 15. PMID:20081198<ref>PMID:20081198</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2k7f" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ab, E]]
[[Category: Ab E]]
[[Category: Bonvin, A]]
[[Category: Bonvin A]]
[[Category: Kobayashi, M]]
[[Category: Kobayashi M]]
[[Category: Siegal, G]]
[[Category: Siegal G]]
[[Category: Activator]]
[[Category: Atp-binding]]
[[Category: Brct]]
[[Category: Complex]]
[[Category: Dna]]
[[Category: Dna replication]]
[[Category: Dna-binding]]
[[Category: Haddock]]
[[Category: Metal-binding]]
[[Category: Model]]
[[Category: Nucleotide-binding]]
[[Category: Nucleus]]
[[Category: Phosphoprotein]]
[[Category: Protein]]
[[Category: Replication-dna complex]]
[[Category: Transcription]]
[[Category: Transcription regulation]]
[[Category: Zinc-finger]]

Latest revision as of 06:44, 1 May 2024

HADDOCK calculated model of the complex between the BRCT region of RFC p140 and dsDNA

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