8ily: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8ily]] is a 2 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=8ILY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ILY FirstGlance]. <br> | <table><tr><td colspan='2'>[[8ily]] is a 2 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=8ILY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ILY FirstGlance]. <br> | ||
</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=8ily FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ily OCA], [https://pdbe.org/8ily PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ily RCSB], [https://www.ebi.ac.uk/pdbsum/8ily PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ily ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</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=8ily FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ily OCA], [https://pdbe.org/8ily PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ily RCSB], [https://www.ebi.ac.uk/pdbsum/8ily PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ily ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/ | [https://www.uniprot.org/uniprot/SET1A_HUMAN SET1A_HUMAN] Histone methyltransferase that specifically methylates 'Lys-4' of histone H3, when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. The non-overalpping localization with SETD1B suggests that SETD1A and SETD1B make non-redundant contributions to the epigenetic control of chromatin structure and gene expression.<ref>PMID:12670868</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Latest revision as of 19:54, 29 May 2024
Crystal structure of the RRM domain of human SETD1A
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