5wxh

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'''Unreleased structure'''
 
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The entry 5wxh is ON HOLD until Paper Publication
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==Crystal structure of TAF3 PHD finger bound to H3K4me3==
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<StructureSection load='5wxh' size='340' side='right' caption='[[5wxh]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5wxh]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WXH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WXH FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5wxg|5wxg]]</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=5wxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wxh OCA], [http://pdbe.org/5wxh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wxh RCSB], [http://www.ebi.ac.uk/pdbsum/5wxh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wxh ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/TAF3_HUMAN TAF3_HUMAN]] Transcription factor TFIID is one of the general factors required for accurate and regulated initiation by RNA polymerase II. TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. Required in complex with TBPL2 for the differentiation of myoblasts into myocytes. The complex replaces TFIID at specific promoters at an early stage in the differentiation process.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Chemical modifications on histones and DNA/RNA constitute a fundamental mechanism for epigenetic regulation. These modifications often function as docking marks to recruit or stabilize cognate "reader" proteins. So far, a platform for quantitative and high-throughput profiling of the epigenetic interactome is urgently needed but still lacking. Here, we report a 3D-carbene chip-based surface plasmon resonance imaging (SPRi) technology for this purpose. The 3D-carbene chip is suitable for immobilizing versatile biomolecules (e.g., peptides, antibody, DNA/RNA) and features low nonspecific binding, random yet function-retaining immobilization, and robustness for reuses. We systematically profiled binding kinetics of 1,000 histone "reader-mark" pairs on a single 3D-carbene chip and validated two recognition events by calorimetric and structural studies. Notably, a discovery on H3K4me3 recognition by the DNA mismatch repair protein MSH6 in Capsella rubella suggests a mechanism of H3K4me3-mediated DNA damage repair in plant.
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Authors:
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Kinetic and high-throughput profiling of epigenetic interactions by 3D-carbene chip-based surface plasmon resonance imaging technology.,Zhao S, Yang M, Zhou W, Zhang B, Cheng Z, Huang J, Zhang M, Wang Z, Wang R, Chen Z, Zhu J, Li H Proc Natl Acad Sci U S A. 2017 Aug 29;114(35):E7245-E7254. doi:, 10.1073/pnas.1704155114. Epub 2017 Aug 14. PMID:28808021<ref>PMID:28808021</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5wxh" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Huang, J]]
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[[Category: Li, H]]
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[[Category: Zhao, S]]
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[[Category: Histone h3]]
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[[Category: Hydrolase]]
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[[Category: Taf3]]

Revision as of 10:45, 13 September 2017

Crystal structure of TAF3 PHD finger bound to H3K4me3

5wxh, resolution 1.30Å

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