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| ==Crystal structure of human Spindlin1 bound to histone H3(K4me3-R8me2a) peptide== | | ==Crystal structure of human Spindlin1 bound to histone H3(K4me3-R8me2a) peptide== |
- | <StructureSection load='4mzf' size='340' side='right' caption='[[4mzf]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='4mzf' size='340' side='right'caption='[[4mzf]], [[Resolution|resolution]] 2.10Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[4mzf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MZF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MZF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4mzf]] is a 2 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=4MZF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MZF FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DA2:NG,NG-DIMETHYL-L-ARGININE'>DA2</scene>, <scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
- | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DA2:NG,NG-DIMETHYL-L-ARGININE'>DA2</scene>, <scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</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=4mzf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mzf OCA], [https://pdbe.org/4mzf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mzf RCSB], [https://www.ebi.ac.uk/pdbsum/4mzf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mzf ProSAT]</span></td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4mzg|4mzg]], [[4mzh|4mzh]]</td></tr>
| + | |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SPIN1, OCR, SPIN ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mzf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mzf OCA], [http://pdbe.org/4mzf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mzf RCSB], [http://www.ebi.ac.uk/pdbsum/4mzf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mzf ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://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). | + | [https://www.uniprot.org/uniprot/H32_HUMAN H32_HUMAN] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| </div> | | </div> |
| <div class="pdbe-citations 4mzf" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4mzf" style="background-color:#fffaf0;"></div> |
| + | |
| + | ==See Also== |
| + | *[[Spindlin|Spindlin]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Human]] | + | [[Category: Homo sapiens]] |
- | [[Category: Ding, X]] | + | [[Category: Large Structures]] |
- | [[Category: Li, H]] | + | [[Category: Ding X]] |
- | [[Category: Su, X]]
| + | [[Category: Li H]] |
- | [[Category: Gene regulation]] | + | [[Category: Su X]] |
- | [[Category: Histone h3]] | + | |
- | [[Category: Nuclear]]
| + | |
- | [[Category: Wnt signal]]
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| Structural highlights
Function
H32_HUMAN
Publication Abstract from PubMed
Histone modification patterns and their combinatorial readout have emerged as a fundamental mechanism for epigenetic regulation. Here we characterized Spindlin1 as a histone effector that senses a cis-tail histone H3 methylation pattern involving trimethyllysine 4 (H3K4me3) and asymmetric dimethylarginine 8 (H3R8me2a) marks. Spindlin1 consists of triple tudor-like Spin/Ssty repeats. Cocrystal structure determination established concurrent recognition of H3K4me3 and H3R8me2a by Spin/Ssty repeats 2 and 1, respectively. Both H3K4me3 and H3R8me2a are recognized using an "insertion cavity" recognition mode, contributing to a methylation state-specific layer of regulation. In vivo functional studies suggest that Spindlin1 activates Wnt/beta-catenin signaling downstream from protein arginine methyltransferase 2 (PRMT2) and the MLL complex, which together are capable of generating a specific H3 "K4me3-R8me2a" pattern. Mutagenesis of Spindlin1 reader pockets impairs activation of Wnt target genes. Taken together, our work connects a histone "lysine-arginine" methylation pattern readout by Spindlin1-to-Wnt signaling at the transcriptional level.
Molecular basis underlying histone H3 lysine-arginine methylation pattern readout by Spin/Ssty repeats of Spindlin1.,Su X, Zhu G, Ding X, Lee SY, Dou Y, Zhu B, Wu W, Li H Genes Dev. 2014 Mar 15;28(6):622-36. doi: 10.1101/gad.233239.113. Epub 2014 Mar, 3. PMID:24589551[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Su X, Zhu G, Ding X, Lee SY, Dou Y, Zhu B, Wu W, Li H. Molecular basis underlying histone H3 lysine-arginine methylation pattern readout by Spin/Ssty repeats of Spindlin1. Genes Dev. 2014 Mar 15;28(6):622-36. doi: 10.1101/gad.233239.113. Epub 2014 Mar, 3. PMID:24589551 doi:http://dx.doi.org/10.1101/gad.233239.113
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