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==Structure of the Epigenetic Oncogene MMSET and inhibition by N-Alkyl Sinefungin Derivatives== | ==Structure of the Epigenetic Oncogene MMSET and inhibition by N-Alkyl Sinefungin Derivatives== | ||
<StructureSection load='5lsx' size='340' side='right' caption='[[5lsx]], [[Resolution|resolution]] 2.90Å' scene=''> | <StructureSection load='5lsx' size='340' side='right'caption='[[5lsx]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5lsx]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LSX OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5lsx]] is a 1 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=5LSX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LSX FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=76O:[(2~{R},5~{S})-1-[(2~{R},3~{S},4~{R},5~{R})-5-(6-AMINOPURIN-9-YL)-3,4-BIS(OXIDANYL)OXOLAN-2-YL]-5-AZANIUMYL-6-OXIDANYL-6-OXIDANYLIDENE-HEXAN-2-YL]-(PHENYLMETHYL)AZANIUM'>76O</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=76O:[(2~{R},5~{S})-1-[(2~{R},3~{S},4~{R},5~{R})-5-(6-AMINOPURIN-9-YL)-3,4-BIS(OXIDANYL)OXOLAN-2-YL]-5-AZANIUMYL-6-OXIDANYL-6-OXIDANYLIDENE-HEXAN-2-YL]-(PHENYLMETHYL)AZANIUM'>76O</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5lsx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lsx OCA], [https://pdbe.org/5lsx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lsx RCSB], [https://www.ebi.ac.uk/pdbsum/5lsx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lsx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/SETD2_HUMAN SETD2_HUMAN] Histone methyltransferase that methylates 'Lys-36' of histone H3. H3 'Lys-36' methylation represents a specific tag for epigenetic transcriptional activation. Probably plays a role in chromatin structure modulation during elongation via its interaction with hyperphosphorylated POLR2A. Binds DNA at promoters. May also act as a transcription activator that binds to promoters. Binds to the promoters of adenovirus 12 E1A gene in case of infection, possibly leading to regulate its expression.<ref>PMID:16118227</ref> | ||
<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 5lsx" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5lsx" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Heightman T]] | ||
[[Category: | [[Category: Pathuri P]] | ||
[[Category: | [[Category: Tisi D]] | ||