7ea8: Difference between revisions

Latest revision as of 13:54, 27 March 2024

Human SETD2 bound to a nucleosome containing oncohistone mutationsHuman SETD2 bound to a nucleosome containing oncohistone mutations

Structural highlights

7ea8 is a 11 chain structure with sequence from Homo sapiens and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.1Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SETD2_HUMAN Histone methyltransferase that methylates 'Lys-36' of histone H3. H3 'Lys-36' methylation represents a specific tag for epigenetic transcriptional activation. Probably plays a role in chromatin structure modulation during elongation via its interaction with hyperphosphorylated POLR2A. Binds DNA at promoters. May also act as a transcription activator that binds to promoters. Binds to the promoters of adenovirus 12 E1A gene in case of infection, possibly leading to regulate its expression.^[1]

References

↑ Sun XJ, Wei J, Wu XY, Hu M, Wang L, Wang HH, Zhang QH, Chen SJ, Huang QH, Chen Z. Identification and characterization of a novel human histone H3 lysine 36-specific methyltransferase. J Biol Chem. 2005 Oct 21;280(42):35261-71. Epub 2005 Aug 22. PMID:16118227 doi:http://dx.doi.org/M504012200

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OCA

[1] Sun XJ, Wei J, Wu XY, Hu M, Wang L, Wang HH, Zhang QH, Chen SJ, Huang QH, Chen Z. Identification and characterization of a novel human histone H3 lysine 36-specific methyltransferase. J Biol Chem. 2005 Oct 21;280(42):35261-71. Epub 2005 Aug 22. PMID:16118227 doi:http://dx.doi.org/M504012200

[1]

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-====
+==Human SETD2 bound to a nucleosome containing oncohistone mutations==
-<StructureSection load='7ea8' size='340' side='right'caption='[[7ea8]]' scene=''>
+<StructureSection load='7ea8' size='340' side='right'caption='[[7ea8]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
+<table><tr><td colspan='2'>[[7ea8]] is a 11 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EA8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EA8 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=7ea8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ea8 OCA], [https://pdbe.org/7ea8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ea8 RCSB], [https://www.ebi.ac.uk/pdbsum/7ea8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ea8 ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=7ea8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ea8 OCA], [https://pdbe.org/7ea8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ea8 RCSB], [https://www.ebi.ac.uk/pdbsum/7ea8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ea8 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/SETD2_HUMAN SETD2_HUMAN] Histone methyltransferase that methylates 'Lys-36' of histone H3. H3 'Lys-36' methylation represents a specific tag for epigenetic transcriptional activation. Probably plays a role in chromatin structure modulation during elongation via its interaction with hyperphosphorylated POLR2A. Binds DNA at promoters. May also act as a transcription activator that binds to promoters. Binds to the promoters of adenovirus 12 E1A gene in case of infection, possibly leading to regulate its expression.<ref>PMID:16118227</ref>
+==See Also==
+*[[Histone 3D structures|Histone 3D structures]]
+*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Z-disk]]
+[[Category: Synthetic construct]]
+[[Category: Jing H]]
+[[Category: Liu Y]]

7ea8: Difference between revisions

Latest revision as of 13:54, 27 March 2024

Human SETD2 bound to a nucleosome containing oncohistone mutationsHuman SETD2 bound to a nucleosome containing oncohistone mutations

Structural highlights

Function

See Also

References

Contents

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7ea8: Difference between revisions

Latest revision as of 13:54, 27 March 2024

Human SETD2 bound to a nucleosome containing oncohistone mutationsHuman SETD2 bound to a nucleosome containing oncohistone mutations

Structural highlights

Function

See Also

References

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

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