7bu9
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Crystal Structure of Spindlin1-H3(K4me3-K9me2) complex== | |
+ | <StructureSection load='7bu9' size='340' side='right'caption='[[7bu9]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[7bu9]] is a 8 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=7BU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BU9 FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.502Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></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=7bu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bu9 OCA], [https://pdbe.org/7bu9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bu9 RCSB], [https://www.ebi.ac.uk/pdbsum/7bu9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bu9 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/SPIN1_HUMAN SPIN1_HUMAN] May play a role in cell-cycle regulation during the transition from gamete to embryo (By similarity). | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Histone recognition by 'reader' modules serves as a fundamental mechanism in epigenetic regulation. Previous studies have shown that Spindlin1 is a reader of histone H3K4me3 as well as "K4me3-R8me2a", and promotes transcription of rDNA or Wnt/TCF4 target genes. Here we show that Spindlin1 also acts as a potent reader of histone H3 "K4me3-K9me3/2" bivalent methylation pattern. Calorimetric titration revealed a binding affinity of 16 nM between Spindlin1 and H3 "K4me3-K9me3" peptide, which is one to three orders of magnitude stronger than most other histone readout events at peptide level. Structural studies revealed concurrent recognition of H3K4me3 and H3K9me3/2 by aromatic pockets 2 and 1 of Spindlin1, respectively. Epigenomic profiling studies showed that Spindlin1 colocalizes with both H3K4me3 and H3K9me3 peaks in a subset of genes enriched in biological processes of transcription and its regulation. Moreover, the distribution of Spindlin1 peaks is primarily associated with H3K4me3 but not H3K9me3, which suggests that Spindlin1 is a downstream effector of H3K4me3 generated in heterochromatic regions. Collectively, our work calls attention to an intriguing function of Spindlin1 as a potent H3 "K4me3-K9me3/2" bivalent mark reader, thereby balancing gene expression and silencing in H3K9me3/2-enriched regions. | ||
- | + | Molecular basis for histone H3 "K4me3-K9me3/2" methylation pattern readout by Spindlin1.,Zhao F, Liu Y, Su X, Lee JE, Song Y, Wang D, Ge K, Gao J, Zhang MQ, Li H J Biol Chem. 2020 Sep 29. pii: RA120.013649. doi: 10.1074/jbc.RA120.013649. PMID:32994220<ref>PMID:32994220</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
- | [[Category: Li | + | <div class="pdbe-citations 7bu9" style="background-color:#fffaf0;"></div> |
- | [[Category: Zhao | + | |
+ | ==See Also== | ||
+ | *[[Spindlin|Spindlin]] | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Homo sapiens]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Li H]] | ||
+ | [[Category: Zhao F]] |
Current revision
Crystal Structure of Spindlin1-H3(K4me3-K9me2) complex
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