2k6g

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Current revision (19:10, 29 May 2024) (edit) (undo)
 
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==Solution structure of the DNA binding BRCT domain from the large subunit of human Replication Factor C==
==Solution structure of the DNA binding BRCT domain from the large subunit of human Replication Factor C==
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<StructureSection load='2k6g' size='340' side='right'caption='[[2k6g]], [[NMR_Ensembles_of_Models | 24 NMR models]]' scene=''>
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<StructureSection load='2k6g' size='340' side='right'caption='[[2k6g]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2k6g]] is a 1 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=2K6G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K6G FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2k6g]] is a 1 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=2K6G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K6G FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2eub|2eub]]</div></td></tr>
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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='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>
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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=2k6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k6g OCA], [https://pdbe.org/2k6g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k6g RCSB], [https://www.ebi.ac.uk/pdbsum/2k6g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k6g 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=2k6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k6g OCA], [https://pdbe.org/2k6g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k6g RCSB], [https://www.ebi.ac.uk/pdbsum/2k6g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k6g ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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>
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[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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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Ab, E]]
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[[Category: Ab E]]
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[[Category: Bonvin, A M.J J]]
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[[Category: Bonvin AMJJ]]
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[[Category: Kobayashi, M]]
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[[Category: Kobayashi M]]
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[[Category: Siegal, G]]
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[[Category: Siegal G]]
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[[Category: Activator]]
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[[Category: Alternative splicing]]
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[[Category: Atp-binding]]
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[[Category: Brct]]
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[[Category: Dna binding]]
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[[Category: Dna binding protein]]
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[[Category: Dna replication]]
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[[Category: Dna-binding]]
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[[Category: Metal-binding]]
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[[Category: Nucleotide-binding]]
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[[Category: Nucleus]]
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[[Category: Phosphoprotein]]
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[[Category: Polymorphism]]
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[[Category: Protein]]
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[[Category: Replication factor c]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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[[Category: Zinc]]
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[[Category: Zinc-finger]]
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Current revision

Solution structure of the DNA binding BRCT domain from the large subunit of human Replication Factor C

PDB ID 2k6g

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