6e2h

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m (Protected "6e2h" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 6e2h is ON HOLD
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==Crystal structure of human Ash2L (SPRY domain and SDI motif) in complex with full length DPY-30==
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<StructureSection load='6e2h' size='340' side='right' caption='[[6e2h]], [[Resolution|resolution]] 2.24&Aring;' scene=''>
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Authors: Joshi, M., Brunzelle, J.S., Couture, J.F.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6e2h]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E2H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E2H FirstGlance]. <br>
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Description: Crystal structure of human Ash2L (SPRY domain and SDI motif) in complex with full length DPY-30
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</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=6e2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e2h OCA], [http://pdbe.org/6e2h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e2h RCSB], [http://www.ebi.ac.uk/pdbsum/6e2h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e2h ProSAT]</span></td></tr>
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[[Category: Unreleased Structures]]
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</table>
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[[Category: Brunzelle, J.S]]
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== Function ==
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[[Category: Couture, J.F]]
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[[http://www.uniprot.org/uniprot/ASH2L_HUMAN ASH2L_HUMAN]] Component of the Set1/Ash2 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3, but not if the neighboring 'Lys-9' residue is already methylated. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. May function as a transcriptional regulator. May play a role in hematopoiesis.<ref>PMID:12670868</ref> <ref>PMID:19556245</ref> [[http://www.uniprot.org/uniprot/DPY30_HUMAN DPY30_HUMAN]] As part of the MLL1/MLL complex, involved in the methylation of histone H3 at 'Lys-4', particularly trimethylation. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. May play some role in histone H3 acetylation. In a teratocarcinoma cell, plays a crucial role in retinoic acid-induced differentiation along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci. May also play an indirect or direct role in endosomal transport.<ref>PMID:19556245</ref> <ref>PMID:19651892</ref> <ref>PMID:21335234</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Brunzelle, J S]]
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[[Category: Couture, J F]]
[[Category: Joshi, M]]
[[Category: Joshi, M]]
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[[Category: Epigenetic]]
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[[Category: Histone]]
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[[Category: Lysine methylation]]
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[[Category: Mll]]
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[[Category: Nucleosome]]
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[[Category: Protein binding]]
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[[Category: Set1]]

Revision as of 21:50, 9 August 2018

Crystal structure of human Ash2L (SPRY domain and SDI motif) in complex with full length DPY-30

6e2h, resolution 2.24Å

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