3qmi

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<StructureSection load='3qmi' size='340' side='right'caption='[[3qmi]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='3qmi' size='340' side='right'caption='[[3qmi]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qmi]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QMI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QMI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qmi]] is a 3 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=3QMI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QMI FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.1&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3qmb|3qmb]], [[3qmc|3qmc]], [[3qmd|3qmd]], [[3qmg|3qmg]], [[3qmh|3qmh]]</div></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=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CFP1, CGBP, CXXC1, PCCX1, PHF18 ([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=3qmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qmi OCA], [https://pdbe.org/3qmi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qmi RCSB], [https://www.ebi.ac.uk/pdbsum/3qmi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qmi 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=3qmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qmi OCA], [https://pdbe.org/3qmi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qmi RCSB], [https://www.ebi.ac.uk/pdbsum/3qmi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qmi ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CXXC1_HUMAN CXXC1_HUMAN]] Transcriptional activator that exhibits a unique DNA binding specificity for CpG unmethylated motifs with a preference for CpGG.<ref>PMID:21407193</ref>
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[https://www.uniprot.org/uniprot/CXXC1_HUMAN CXXC1_HUMAN] Transcriptional activator that exhibits a unique DNA binding specificity for CpG unmethylated motifs with a preference for CpGG.<ref>PMID:21407193</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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CFP1 is a CXXC domain-containing protein and an essential component of the SETD1 histone H3K4 methyltransferase complex. CXXC domain proteins direct different chromatin-modifying activities to various chromatin regions. Here, we report crystal structures of the CFP1 CXXC domain in complex with six different CpG DNA sequences. The crescent-shaped CFP1 CXXC domain is wedged into the major groove of the CpG DNA, distorting the B-form DNA, and interacts extensively with the major groove of the DNA. The structures elucidate the molecular mechanism of the non-methylated CpG-binding specificity of the CFP1 CXXC domain. The CpG motif is confined by a tripeptide located in a rigid loop, which only allows the accommodation of the non-methylated CpG dinucleotide. Furthermore, we demonstrate that CFP1 has a preference for a guanosine nucleotide following the CpG motif.
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The structural basis for selective binding of non-methylated CpG islands by the CFP1 CXXC domain.,Xu C, Bian C, Lam R, Dong A, Min J Nat Commun. 2011 Mar;2:227. PMID:21407193<ref>PMID:21407193</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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<div class="pdbe-citations 3qmi" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__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: Arrowsmith, C H]]
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[[Category: Arrowsmith CH]]
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[[Category: Bian, C]]
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[[Category: Bian C]]
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[[Category: Bountra, C]]
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[[Category: Bountra C]]
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[[Category: Edwards, A M]]
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[[Category: Edwards AM]]
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[[Category: MacKenzie, F]]
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[[Category: MacKenzie F]]
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[[Category: Min, J]]
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[[Category: Min J]]
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[[Category: Structural genomic]]
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[[Category: Weigelt J]]
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[[Category: Weigelt, J]]
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[[Category: Xu C]]
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[[Category: Xu, C]]
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[[Category: Dna binding]]
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[[Category: Dna binding protein-dna complex]]
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[[Category: Sgc]]
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Current revision

Structural Basis of Selective Binding of Non-Methylated CpG islands (DNA-ACGT) by the CXXC Domain of CFP1

PDB ID 3qmi

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