3p8h
From Proteopedia
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{{STRUCTURE_3p8h| PDB=3p8h | SCENE= }} | {{STRUCTURE_3p8h| PDB=3p8h | SCENE= }} | ||
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===Crystal structure of L3MBTL1 (MBT repeat) in complex with a nicotinamide antagonist=== | ===Crystal structure of L3MBTL1 (MBT repeat) in complex with a nicotinamide antagonist=== | ||
| + | {{ABSTRACT_PUBMED_21417280}} | ||
| - | + | ==Function== | |
| - | + | [[http://www.uniprot.org/uniprot/LMBL1_HUMAN LMBL1_HUMAN]] Polycomb group (PcG) protein that specifically recognizes and binds mono- and dimethyllysine residues on target proteins, therey acting as a 'reader' of a network of post-translational modifications. PcG proteins maintain the transcriptionally repressive state of genes: acts as a chromatin compaction factor by recognizing and binding mono- and dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condense chromatin and repress transcription. Recognizes and binds p53/TP53 monomethylated at 'Lys-382', leading to repress p53/TP53-target genes. Also recognizes and binds RB1/RB monomethylated at 'Lys-860'. Participates in the ETV6-mediated repression. Probably plays a role in cell proliferation. Overexpression induces multinucleated cells, suggesting that it is required to accomplish normal mitosis.<ref>PMID:17540172</ref> <ref>PMID:18408754</ref> <ref>PMID:20870719</ref> <ref>PMID:20870725</ref> | |
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==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:021417280</ref><references group="xtra"/> | + | <ref group="xtra">PMID:021417280</ref><references group="xtra"/><references/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Arrowsmith, C H.]] | [[Category: Arrowsmith, C H.]] | ||
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[[Category: Vedadi, M.]] | [[Category: Vedadi, M.]] | ||
[[Category: Weigelt, J.]] | [[Category: Weigelt, J.]] | ||
| + | [[Category: Mbt repeat]] | ||
| + | [[Category: Methylated lysines on histone protein]] | ||
| + | [[Category: Sgc]] | ||
| + | [[Category: Structural genomics consortium]] | ||
| + | [[Category: Transcription]] | ||
| + | [[Category: Transcriptional repression]] | ||
Revision as of 08:22, 2 May 2013
Contents |
Crystal structure of L3MBTL1 (MBT repeat) in complex with a nicotinamide antagonist
Template:ABSTRACT PUBMED 21417280
Function
[LMBL1_HUMAN] Polycomb group (PcG) protein that specifically recognizes and binds mono- and dimethyllysine residues on target proteins, therey acting as a 'reader' of a network of post-translational modifications. PcG proteins maintain the transcriptionally repressive state of genes: acts as a chromatin compaction factor by recognizing and binding mono- and dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condense chromatin and repress transcription. Recognizes and binds p53/TP53 monomethylated at 'Lys-382', leading to repress p53/TP53-target genes. Also recognizes and binds RB1/RB monomethylated at 'Lys-860'. Participates in the ETV6-mediated repression. Probably plays a role in cell proliferation. Overexpression induces multinucleated cells, suggesting that it is required to accomplish normal mitosis.[1] [2] [3] [4]
About this Structure
3p8h is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Herold JM, Wigle TJ, Norris JL, Lam R, Korboukh VK, Gao C, Ingerman LA, Kireev DB, Senisterra G, Vedadi M, Tripathy A, Brown PJ, Arrowsmith CH, Jin J, Janzen WP, Frye SV. Small-molecule ligands of methyl-lysine binding proteins. J Med Chem. 2011 Apr 14;54(7):2504-11. Epub 2011 Mar 18. PMID:21417280 doi:10.1021/jm200045v
- ↑ Trojer P, Li G, Sims RJ 3rd, Vaquero A, Kalakonda N, Boccuni P, Lee D, Erdjument-Bromage H, Tempst P, Nimer SD, Wang YH, Reinberg D. L3MBTL1, a histone-methylation-dependent chromatin lock. Cell. 2007 Jun 1;129(5):915-28. PMID:17540172 doi:10.1016/j.cell.2007.03.048
- ↑ Kalakonda N, Fischle W, Boccuni P, Gurvich N, Hoya-Arias R, Zhao X, Miyata Y, Macgrogan D, Zhang J, Sims JK, Rice JC, Nimer SD. Histone H4 lysine 20 monomethylation promotes transcriptional repression by L3MBTL1. Oncogene. 2008 Jul 17;27(31):4293-304. doi: 10.1038/onc.2008.67. Epub 2008 Apr, 14. PMID:18408754 doi:10.1038/onc.2008.67
- ↑ Saddic LA, West LE, Aslanian A, Yates JR 3rd, Rubin SM, Gozani O, Sage J. Methylation of the retinoblastoma tumor suppressor by SMYD2. J Biol Chem. 2010 Nov 26;285(48):37733-40. doi: 10.1074/jbc.M110.137612. Epub, 2010 Sep 24. PMID:20870719 doi:10.1074/jbc.M110.137612
- ↑ West LE, Roy S, Lachmi-Weiner K, Hayashi R, Shi X, Appella E, Kutateladze TG, Gozani O. The MBT repeats of L3MBTL1 link set8 mediated p53 methylation at lysine 382 to target gene repression. J Biol Chem. 2010 Sep 24. PMID:20870725 doi:10.1074/jbc.M110.139527
Categories: Homo sapiens | Arrowsmith, C H. | Bountra, C. | Brown, P J. | Edwards, A M. | Frye, S V. | Gao, C. | Herold, J M. | Kireev, D. | Lam, R. | Ouyang, H. | Ravichandran, M. | SGC, Structural Genomics Consortium. | Senisterra, G. | Tempel, W. | Vedadi, M. | Weigelt, J. | Mbt repeat | Methylated lysines on histone protein | Sgc | Structural genomics consortium | Transcription | Transcriptional repression
