5y5w

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'''Unreleased structure'''
 
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The entry 5y5w is ON HOLD
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==Crystal structure of human Spindlin1 in complex with a histone H4K20(me3) peptide==
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<StructureSection load='5y5w' size='340' side='right'caption='[[5y5w]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5y5w]] is a 7 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=5Y5W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y5W 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=M3L:N-TRIMETHYLLYSINE'>M3L</scene></td></tr>
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<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=5y5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y5w OCA], [http://pdbe.org/5y5w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y5w RCSB], [http://www.ebi.ac.uk/pdbsum/5y5w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y5w ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[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).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Using methods combining cross-linking, pull-down assays, and stable isotope labeling by amino acids in cell culture with mass spectrometry, we identified that the Tudor domain-containing protein Spindlin-1 recognizes trimethylation of histone H4 lysine 20 (H4K20me3). The binding affinity of Spindlin-1 to H4K20me3 is weaker than that to H3K4me3, indicating H4K20me3 as a secondary substrate for Spindlin-1. Structural studies of Spindlin-1 in complex with the H4K20me3 peptide indicate that Spindlin-1 attains a distinct binding mode for H4K20me3 recognition. Further biochemical analysis identified that Spindlin-1 also binds methylated R23 of H4, providing new clues for the function of Spindlin-1.
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Authors: Wang, C.L., Zang, J.Y.
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Spindlin-1 recognizes methylations of K20 and R23 of histone H4 tail.,Wang C, Zhan L, Wu M, Ma R, Yao J, Xiong Y, Pan Y, Guan S, Zhang X, Zang J FEBS Lett. 2018 Dec;592(24):4098-4110. doi: 10.1002/1873-3468.13281. Epub 2018, Nov 17. PMID:30381828<ref>PMID:30381828</ref>
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Description: Crystal structure of human Spindlin1 in complex with a histone H4K20(me3) peptide
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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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[[Category: Wang, C.L]]
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<div class="pdbe-citations 5y5w" style="background-color:#fffaf0;"></div>
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[[Category: Zang, J.Y]]
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==See Also==
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*[[Spindlin|Spindlin]]
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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: Human]]
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[[Category: Large Structures]]
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[[Category: Wang, C]]
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[[Category: Zang, J]]
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[[Category: Gene regulation]]
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[[Category: Histone]]
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[[Category: Reader]]

Revision as of 08:17, 20 March 2019

Crystal structure of human Spindlin1 in complex with a histone H4K20(me3) peptide

PDB ID 5y5w

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