5y5w: Difference between revisions
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The | ==Crystal structure of human Spindlin1 in complex with a histone H4K20(me3) peptide== | ||
<StructureSection load='5y5w' size='340' side='right'caption='[[5y5w]], [[Resolution|resolution]] 3.30Å' scene=''> | |||
== Structural highlights == | |||
<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> | |||
</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> | |||
<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> | |||
<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> | |||
</table> | |||
== 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). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Wang, C | <div class="pdbe-citations 5y5w" style="background-color:#fffaf0;"></div> | ||
[[Category: Zang, J | |||
==See Also== | |||
*[[Spindlin|Spindlin]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Human]] | |||
[[Category: Large Structures]] | |||
[[Category: Wang, C]] | |||
[[Category: Zang, J]] | |||
[[Category: Gene regulation]] | |||
[[Category: Histone]] | |||
[[Category: Reader]] | |||
Revision as of 08:17, 20 March 2019
Crystal structure of human Spindlin1 in complex with a histone H4K20(me3) peptide
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