5c0m
From Proteopedia
(Difference between revisions)
m (Protected "5c0m" [edit=sysop:move=sysop]) |
|||
(4 intermediate revisions not shown.) | |||
Line 1: | Line 1: | ||
- | '''Unreleased structure''' | ||
- | + | ==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=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[5c0m]] is a 4 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=5C0M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C0M 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]] 1.6Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4WQ:(2S)-2-AMINO-7,7-DIMETHYLOCTANOIC+ACID'>4WQ</scene>, <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5c0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c0m OCA], [https://pdbe.org/5c0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c0m RCSB], [https://www.ebi.ac.uk/pdbsum/5c0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c0m ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://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> | |
- | [[Category: | + | </div> |
- | [[Category: | + | <div class="pdbe-citations 5c0m" style="background-color:#fffaf0;"></div> |
- | [[Category: | + | |
- | [[Category: Bountra | + | ==See Also== |
- | [[Category: | + | *[[SAGA-associated factor|SAGA-associated factor]] |
- | [[Category: | + | == References == |
- | [[Category: | + | <references/> |
- | [[Category: | + | __TOC__ |
- | [[Category: | + | </StructureSection> |
- | [[Category: | + | [[Category: Homo sapiens]] |
+ | [[Category: Large Structures]] | ||
+ | [[Category: Arrowsmith CH]] | ||
+ | [[Category: Bountra C]] | ||
+ | [[Category: Cerovina T]] | ||
+ | [[Category: Dong A]] | ||
+ | [[Category: Edwards AM]] | ||
+ | [[Category: Min J]] | ||
+ | [[Category: Tempel W]] | ||
+ | [[Category: Xu C]] |
Current revision
Crystal structure of SGF29 tandem tudor domain in complex with a Carba containing peptide
|
Categories: Homo sapiens | Large Structures | Arrowsmith CH | Bountra C | Cerovina T | Dong A | Edwards AM | Min J | Tempel W | Xu C