5c0m
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| + | |||
==Crystal structure of SGF29 tandem tudor domain in complex with a Carba containing peptide== | ==Crystal structure of SGF29 tandem tudor domain in complex with a Carba containing peptide== | ||
<StructureSection load='5c0m' size='340' side='right' caption='[[5c0m]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='5c0m' size='340' side='right' caption='[[5c0m]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
| Line 5: | Line 6: | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=4WQ:(2S)-2-AMINO-7,7-DIMETHYLOCTANOIC+ACID'>4WQ</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=4WQ:(2S)-2-AMINO-7,7-DIMETHYLOCTANOIC+ACID'>4WQ</scene></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=5c0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c0m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5c0m RCSB], [http://www.ebi.ac.uk/pdbsum/5c0m PDBsum]</span></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=5c0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c0m OCA], [http://pdbe.org/5c0m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c0m RCSB], [http://www.ebi.ac.uk/pdbsum/5c0m PDBsum]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/SGF29_HUMAN SGF29_HUMAN]] Involved in transcriptional regulation, through association with histone acetyltransferase (HAT) SAGA-type complexes like the TFTC-HAT, ATAC or STAGA complexes. Specifically recognizes and binds methylated 'Lys-4' of histone H3 (H3K4me), with a preference for trimethylated form (H3K4me3). In the SAGA-type complexes, required to recruit complexes to H3K4me. May be involved in MYC-mediated oncogenic transformation.<ref>PMID:19103755</ref> | [[http://www.uniprot.org/uniprot/SGF29_HUMAN SGF29_HUMAN]] Involved in transcriptional regulation, through association with histone acetyltransferase (HAT) SAGA-type complexes like the TFTC-HAT, ATAC or STAGA complexes. Specifically recognizes and binds methylated 'Lys-4' of histone H3 (H3K4me), with a preference for trimethylated form (H3K4me3). In the SAGA-type complexes, required to recruit complexes to H3K4me. May be involved in MYC-mediated oncogenic transformation.<ref>PMID:19103755</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | A large number of structurally diverse epigenetic reader proteins specifically recognize methylated lysine residues on histone proteins. Here we describe comparative thermodynamic, structural and computational studies on recognition of the positively charged natural trimethyllysine and its neutral analogues by reader proteins. This work provides experimental and theoretical evidence that reader proteins predominantly recognize trimethyllysine via a combination of favourable cation-pi interactions and the release of the high-energy water molecules that occupy the aromatic cage of reader proteins on the association with the trimethyllysine side chain. These results have implications in rational drug design by specifically targeting the aromatic cage of readers of trimethyllysine. | ||
| + | |||
| + | Chemical basis for the recognition of trimethyllysine by epigenetic reader proteins.,Kamps JJ, Huang J, Poater J, Xu C, Pieters BJ, Dong A, Min J, Sherman W, Beuming T, Matthias Bickelhaupt F, Li H, Mecinovic J Nat Commun. 2015 Nov 18;6:8911. doi: 10.1038/ncomms9911. PMID:26578293<ref>PMID:26578293</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5c0m" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 19:10, 10 May 2016
Crystal structure of SGF29 tandem tudor domain in complex with a Carba containing peptide
| |||||||||||
