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3olc

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==Crystal structure of the N-terminal region of TopBP1==
==Crystal structure of the N-terminal region of TopBP1==
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<StructureSection load='3olc' size='340' side='right' caption='[[3olc]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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<StructureSection load='3olc' size='340' side='right'caption='[[3olc]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3olc]] is a 1 chain structure with 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=3OLC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OLC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3olc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OLC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OLC FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TOPBP1, KIAA0259 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3olc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3olc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3olc RCSB], [http://www.ebi.ac.uk/pdbsum/3olc PDBsum]</span></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=3olc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3olc OCA], [https://pdbe.org/3olc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3olc RCSB], [https://www.ebi.ac.uk/pdbsum/3olc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3olc ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/TOPB1_HUMAN TOPB1_HUMAN] Required for DNA replication. Plays a role in the rescue of stalled replication forks and checkpoint control. Binds double-stranded DNA breaks and nicks as well as single-stranded DNA. Recruits the SWI/SNF chromatin remodeling complex to E2F1-responsive promoters. Down-regulates E2F1 activity and inhibits E2F1-dependent apoptosis during G1/S transition and after DNA damage. Induces a large increase in the kinase activity of ATR.<ref>PMID:10498869</ref> <ref>PMID:11395493</ref> <ref>PMID:11714696</ref> <ref>PMID:12697828</ref> <ref>PMID:15075294</ref> <ref>PMID:16530042</ref>
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Human DNA Topoisomerase IIbeta binding protein 1 (TopBP1) is a modulating protein that plays an essential role in the response to DNA damage. The N-terminal region of TopBP1, which contains predicted BRCA1-carboxy terminal (BRCT) domains 1 and 2, binds to Rad9, a component of the cell cycle checkpoint clamp Rad9-Hus1-Rad1 complex. Here, we report the crystal structure of the TopBP1N-terminal region (residues 1-290) at 2.4A resolution. Interestingly, in addition to the predicted tandem BRCT1-2 repeats (residues 103-284), residues 7-98 form a previously unreported BRCT domain (here, BRCT0). In contrast to both BRCT1 and BRCT2, which possess the conventional phosphopeptide binding residues within a surface pocket, the corresponding pocket in BRCT0 is largely hydrophobic. Structural comparisons together with peptide binding studies indicate that the tandem BRCT1-2 domains are the binding region for phosphorylated Ser387 in Rad9.
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Crystal structure of the N-terminal region of human Topoisomerase IIbeta binding protein 1.,Huo YG, Bai L, Xu M, Jiang T Biochem Biophys Res Commun. 2010 Oct 22;401(3):401-5. Epub 2010 Sep 19. PMID:20858457<ref>PMID:20858457</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==See Also==
==See Also==
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Bai, L]]
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[[Category: Large Structures]]
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[[Category: Huo, Y G]]
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[[Category: Bai L]]
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[[Category: Jiang, T]]
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[[Category: Huo YG]]
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[[Category: Xu, M]]
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[[Category: Jiang T]]
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[[Category: Brct domain]]
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[[Category: Xu M]]
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[[Category: Dna binding protein]]
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[[Category: Dna repair]]
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[[Category: Rad9]]
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Current revision

Crystal structure of the N-terminal region of TopBP1

PDB ID 3olc

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