4rt4: Difference between revisions

Revision as of 13:42, 7 October 2015

Crystal structure of Dpy30 complexed with Bre2

Structural highlights

4rt4 is a 5 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[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.^[1] ^[2] ^[3] [BRE2_YEAST] The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.^[4] ^[5]

References

↑ Patel A, Dharmarajan V, Vought VE, Cosgrove MS. On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complex. J Biol Chem. 2009 Sep 4;284(36):24242-56. Epub 2009 Jun 25. PMID:19556245 doi:M109.014498
↑ Xu Z, Gong Q, Xia B, Groves B, Zimmermann M, Mugler C, Mu D, Matsumoto B, Seaman M, Ma D. A role of histone H3 lysine 4 methyltransferase components in endosomal trafficking. J Cell Biol. 2009 Aug 10;186(3):343-53. doi: 10.1083/jcb.200902146. Epub 2009 Aug, 3. PMID:19651892 doi:https://dx.doi.org/10.1083/jcb.200902146
↑ Jiang H, Shukla A, Wang X, Chen WY, Bernstein BE, Roeder RG. Role for Dpy-30 in ES cell-fate specification by regulation of H3K4 methylation within bivalent domains. Cell. 2011 Feb 18;144(4):513-25. doi: 10.1016/j.cell.2011.01.020. PMID:21335234 doi:https://dx.doi.org/10.1016/j.cell.2011.01.020
↑ Roguev A, Schaft D, Shevchenko A, Pijnappel WW, Wilm M, Aasland R, Stewart AF. The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4. EMBO J. 2001 Dec 17;20(24):7137-48. PMID:11742990 doi:https://dx.doi.org/10.1093/emboj/20.24.7137
↑ Krogan NJ, Dover J, Khorrami S, Greenblatt JF, Schneider J, Johnston M, Shilatifard A. COMPASS, a histone H3 (Lysine 4) methyltransferase required for telomeric silencing of gene expression. J Biol Chem. 2002 Mar 29;277(13):10753-5. Epub 2002 Jan 22. PMID:11805083 doi:https://dx.doi.org/10.1074/jbc.C200023200

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OCA

[1] Patel A, Dharmarajan V, Vought VE, Cosgrove MS. On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complex. J Biol Chem. 2009 Sep 4;284(36):24242-56. Epub 2009 Jun 25. PMID:19556245 doi:M109.014498

[2] Xu Z, Gong Q, Xia B, Groves B, Zimmermann M, Mugler C, Mu D, Matsumoto B, Seaman M, Ma D. A role of histone H3 lysine 4 methyltransferase components in endosomal trafficking. J Cell Biol. 2009 Aug 10;186(3):343-53. doi: 10.1083/jcb.200902146. Epub 2009 Aug, 3. PMID:19651892 doi:https://dx.doi.org/10.1083/jcb.200902146

[3] Jiang H, Shukla A, Wang X, Chen WY, Bernstein BE, Roeder RG. Role for Dpy-30 in ES cell-fate specification by regulation of H3K4 methylation within bivalent domains. Cell. 2011 Feb 18;144(4):513-25. doi: 10.1016/j.cell.2011.01.020. PMID:21335234 doi:https://dx.doi.org/10.1016/j.cell.2011.01.020

[4] Roguev A, Schaft D, Shevchenko A, Pijnappel WW, Wilm M, Aasland R, Stewart AF. The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4. EMBO J. 2001 Dec 17;20(24):7137-48. PMID:11742990 doi:https://dx.doi.org/10.1093/emboj/20.24.7137

[5] Krogan NJ, Dover J, Khorrami S, Greenblatt JF, Schneider J, Johnston M, Shilatifard A. COMPASS, a histone H3 (Lysine 4) methyltransferase required for telomeric silencing of gene expression. J Biol Chem. 2002 Mar 29;277(13):10753-5. Epub 2002 Jan 22. PMID:11805083 doi:https://dx.doi.org/10.1074/jbc.C200023200

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Crystal structure of Dpy30 complexed with Bre2==
+<StructureSection load='4rt4' size='340' side='right' caption='[[4rt4]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-The entry 4rt4 is ON HOLD  until Paper Publication
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4rt4]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RT4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RT4 FirstGlance]. <br>
-Authors: Zhang, H.M., Li, M., Chang, W.R.
+</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=4rt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rt4 OCA], [http://pdbe.org/4rt4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rt4 RCSB], [http://www.ebi.ac.uk/pdbsum/4rt4 PDBsum]</span></td></tr>
+</table>
-Description: Crystal structure of Dpy30 complexed with Bre2
+== Function ==
-[[Category: Unreleased Structures]]
+[[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>  [[http://www.uniprot.org/uniprot/BRE2_YEAST BRE2_YEAST]] The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.<ref>PMID:11742990</ref> <ref>PMID:11805083</ref>
-[[Category: Zhang, H.M]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Chang, W R]]
 [[Category: Li, M]]
-[[Category: Chang, W.R]]
+[[Category: Zhang, H M]]
+[[Category: H3k4 methylation]]
+[[Category: Protein binding]]
+[[Category: X-type helix]]

4rt4: Difference between revisions

Revision as of 13:42, 7 October 2015

Crystal structure of Dpy30 complexed with Bre2

Structural highlights

Function

References

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