5qt2: Difference between revisions

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New page: '''Unreleased structure''' The entry 5qt2 is ON HOLD Authors: Harding, R.J., Tempel, W., DOUANGAMATH, A., BRANDAO-NETO, J., Collins, P.M., Krojer, T., Mader, P., Schapira, M., von Delft...
 
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'''Unreleased structure'''


The entry 5qt2 is ON HOLD
==PanDDA analysis group deposition -- Partial occupancy interpretation of PanDDA event map: SETDB1 in complex with FMOPL000074a==
 
<StructureSection load='5qt2' size='340' side='right'caption='[[5qt2]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
Authors: Harding, R.J., Tempel, W., DOUANGAMATH, A., BRANDAO-NETO, J., Collins, P.M., Krojer, T., Mader, P., Schapira, M., von Delft, F., Bountra, C., Edwards, A.M., Arrowsmith, C.H., Santhakumar, V.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5qt2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5QT2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5QT2 FirstGlance]. <br>
Description: PanDDA analysis group deposition --Partial occupancy interpretation of PanDDA event map: SETDB1 in complex with FMOPL000074a
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.59&#8491;</td></tr>
[[Category: Unreleased Structures]]
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AW7:2-[4-(1~{H}-pyrazol-3-yl)phenoxy]pyrimidine'>AW7</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
[[Category: Schapira, M]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5qt2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5qt2 OCA], [https://pdbe.org/5qt2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5qt2 RCSB], [https://www.ebi.ac.uk/pdbsum/5qt2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5qt2 ProSAT]</span></td></tr>
[[Category: Edwards, A.M]]
</table>
[[Category: Arrowsmith, C.H]]
== Function ==
[[Category: Brandao-Neto, J]]
[https://www.uniprot.org/uniprot/SETB1_HUMAN SETB1_HUMAN] Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. H3 'Lys-9' trimethylation is coordinated with DNA methylation. Probably forms a complex with MBD1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Its activity is dependent on MBD1 and is heritably maintained through DNA replication by being recruited by CAF-1. SETDB1 is targeted to histone H3 by TRIM28/TIF1B, a factor recruited by KRAB zinc-finger proteins.<ref>PMID:12869583</ref> <ref>PMID:14536086</ref> <ref>PMID:15327775</ref> <ref>PMID:17952062</ref>
[[Category: Santhakumar, V]]
== References ==
[[Category: Collins, P.M]]
<references/>
[[Category: Douangamath, A]]
__TOC__
[[Category: Mader, P]]
</StructureSection>
[[Category: Krojer, T]]
[[Category: Homo sapiens]]
[[Category: Harding, R.J]]
[[Category: Large Structures]]
[[Category: Von Delft, F]]
[[Category: Arrowsmith CH]]
[[Category: Bountra, C]]
[[Category: BRANDAO-NETO J]]
[[Category: Tempel, W]]
[[Category: Bountra C]]
[[Category: Collins PM]]
[[Category: DOUANGAMATH A]]
[[Category: Edwards AM]]
[[Category: Harding RJ]]
[[Category: Krojer T]]
[[Category: Mader P]]
[[Category: Santhakumar V]]
[[Category: Schapira M]]
[[Category: Tempel W]]
[[Category: Von Delft F]]

Latest revision as of 14:27, 21 February 2024

PanDDA analysis group deposition -- Partial occupancy interpretation of PanDDA event map: SETDB1 in complex with FMOPL000074aPanDDA analysis group deposition -- Partial occupancy interpretation of PanDDA event map: SETDB1 in complex with FMOPL000074a

Structural highlights

5qt2 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.59Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SETB1_HUMAN Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. H3 'Lys-9' trimethylation is coordinated with DNA methylation. Probably forms a complex with MBD1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Its activity is dependent on MBD1 and is heritably maintained through DNA replication by being recruited by CAF-1. SETDB1 is targeted to histone H3 by TRIM28/TIF1B, a factor recruited by KRAB zinc-finger proteins.[1] [2] [3] [4]

References

  1. ↑ Ayyanathan K, Lechner MS, Bell P, Maul GG, Schultz DC, Yamada Y, Tanaka K, Torigoe K, Rauscher FJ 3rd. Regulated recruitment of HP1 to a euchromatic gene induces mitotically heritable, epigenetic gene silencing: a mammalian cell culture model of gene variegation. Genes Dev. 2003 Aug 1;17(15):1855-69. Epub 2003 Jul 17. PMID:12869583 doi:http://dx.doi.org/10.1101/gad.1102803
  2. ↑ Wang H, An W, Cao R, Xia L, Erdjument-Bromage H, Chatton B, Tempst P, Roeder RG, Zhang Y. mAM facilitates conversion by ESET of dimethyl to trimethyl lysine 9 of histone H3 to cause transcriptional repression. Mol Cell. 2003 Aug;12(2):475-87. PMID:14536086
  3. ↑ Sarraf SA, Stancheva I. Methyl-CpG binding protein MBD1 couples histone H3 methylation at lysine 9 by SETDB1 to DNA replication and chromatin assembly. Mol Cell. 2004 Aug 27;15(4):595-605. PMID:15327775 doi:http://dx.doi.org/10.1016/j.molcel.2004.06.043
  4. ↑ Takada I, Mihara M, Suzawa M, Ohtake F, Kobayashi S, Igarashi M, Youn MY, Takeyama K, Nakamura T, Mezaki Y, Takezawa S, Yogiashi Y, Kitagawa H, Yamada G, Takada S, Minami Y, Shibuya H, Matsumoto K, Kato S. A histone lysine methyltransferase activated by non-canonical Wnt signalling suppresses PPAR-gamma transactivation. Nat Cell Biol. 2007 Nov;9(11):1273-85. Epub 2007 Oct 21. PMID:17952062 doi:http://dx.doi.org/10.1038/ncb1647

5qt2, resolution 1.59Å

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