5ccm: Difference between revisions

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'''Unreleased structure'''
==Crystal structure of SMYD3 with SAM and EPZ030456==
 
<StructureSection load='5ccm' size='340' side='right' caption='[[5ccm]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
The entry 5ccm is ON HOLD  until Paper Publication
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5ccm]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CCM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CCM FirstGlance]. <br>
Authors: Boriack-Sjodin, P.A.
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4ZX:6-CHLORANYL-2-OXIDANYLIDENE-N-[(1S,5R)-8-[4-[(PHENYLMETHYL)AMINO]PIPERIDIN-1-YL]SULFONYL-8-AZABICYCLO[3.2.1]OCTAN-3-YL]-1,3-DIHYDROINDOLE-5-CARBOXAMIDE'>4ZX</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ccl|5ccl]]</td></tr>
Description: Crystal structure of SMYD3 with SAM and EPZ030456
<tr id='activity'><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>
[[Category: Unreleased Structures]]
<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=5ccm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ccm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5ccm RCSB], [http://www.ebi.ac.uk/pdbsum/5ccm PDBsum]</span></td></tr>
[[Category: Boriack-Sjodin, P.A]]
</table>
== Function ==
[[http://www.uniprot.org/uniprot/SMYD3_HUMAN SMYD3_HUMAN]] Histone methyltransferase. Specifically methylates 'Lys-4' and 'Lys-5' of histone H3, inducing di- and tri-methylation, but not monomethylation. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences.<ref>PMID:15235609</ref> <ref>PMID:22419068</ref> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Histone-lysine N-methyltransferase]]
[[Category: Boriack-Sjodin, P A]]
[[Category: Drug discovery]]
[[Category: Epigenetic]]
[[Category: Methyltransferase]]
[[Category: Protein-inhibitor complex]]
[[Category: Transferase-transferase inhibitor complex]]

Revision as of 14:23, 9 September 2015

Crystal structure of SMYD3 with SAM and EPZ030456Crystal structure of SMYD3 with SAM and EPZ030456

Structural highlights

5ccm is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Activity:Histone-lysine N-methyltransferase, with EC number 2.1.1.43
Resources:FirstGlance, OCA, RCSB, PDBsum

Function

[SMYD3_HUMAN] Histone methyltransferase. Specifically methylates 'Lys-4' and 'Lys-5' of histone H3, inducing di- and tri-methylation, but not monomethylation. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences.[1] [2]

References

  1. ↑ Hamamoto R, Furukawa Y, Morita M, Iimura Y, Silva FP, Li M, Yagyu R, Nakamura Y. SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells. Nat Cell Biol. 2004 Aug;6(8):731-40. Epub 2004 Jul 4. PMID:15235609 doi:10.1038/ncb1151
  2. ↑ Van Aller GS, Reynoird N, Barbash O, Huddleston M, Liu S, Zmoos AF, McDevitt P, Sinnamon R, Le B, Mas G, Annan R, Sage J, Garcia BA, Tummino PJ, Gozani O, Kruger RG. Smyd3 regulates cancer cell phenotypes and catalyzes histone H4 lysine 5 methylation. Epigenetics. 2012 Apr;7(4):340-3. doi: 10.4161/epi.19506. Epub 2012 Apr 1. PMID:22419068 doi:10.4161/epi.19506

5ccm, resolution 2.30Å

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