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4erq
From Proteopedia
(Difference between revisions)
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| - | + | ==X-ray structure of WDR5-MLL2 Win motif peptide binary complex== | |
| - | + | <StructureSection load='4erq' size='340' side='right' caption='[[4erq]], [[Resolution|resolution]] 1.91Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4erq]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ERQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ERQ FirstGlance]. <br> | |
| - | + | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ery|4ery]], [[4erz|4erz]], [[4es0|4es0]], [[4esg|4esg]]</td></tr> | |
| - | + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BIG3, WDR5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | |
| - | + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </span></td></tr> | |
| - | + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4erq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4erq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4erq RCSB], [http://www.ebi.ac.uk/pdbsum/4erq PDBsum]</span></td></tr> | |
| - | + | <table> | |
| - | + | == Disease == | |
| - | + | [[http://www.uniprot.org/uniprot/MLL2_HUMAN MLL2_HUMAN]] Kabuki syndrome. The disease is caused by mutations affecting the gene represented in this entry. | |
| - | + | == Function == | |
| - | + | [[http://www.uniprot.org/uniprot/WDR5_HUMAN WDR5_HUMAN]] Contributes to histone modification. May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4'. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. May regulate osteoblasts differentiation.<ref>PMID:19556245</ref> <ref>PMID:19103755</ref> <ref>PMID:20018852</ref> <ref>PMID:16600877</ref> <ref>PMID:16829960</ref> [[http://www.uniprot.org/uniprot/MLL2_HUMAN MLL2_HUMAN]] Histone methyltransferase. Methylates 'Lys-4' of histone H3 (H3K4me). H3K4me represents a specific tag for epigenetic transcriptional activation. Acts as a coactivator for estrogen receptor by being recruited by ESR1, thereby activating transcription.<ref>PMID:16603732</ref> <ref>PMID:17500065</ref> <ref>PMID:17851529</ref> | |
| - | == | + | == References == |
| - | [[4erq]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ERQ OCA]. | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Histone-lysine N-methyltransferase]] | [[Category: Histone-lysine N-methyltransferase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
Revision as of 08:01, 5 June 2014
X-ray structure of WDR5-MLL2 Win motif peptide binary complex
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Categories: Histone-lysine N-methyltransferase | Homo sapiens | Cosgrove, M S. | Dharmarajan, V. | Lee, J H. | Patel, A. | Skalnik, D G. | 3-10 helix | Ash2l | Beta propeller | Core complex | Histone | Lysine methyltransferase | Mll1 | Rbbp5 | Transcription-transferase complex | Wd40 | Win motif peptide
