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| | ==The MBT repeats of human SCML2 in a complex with histone H2A peptide== | | ==The MBT repeats of human SCML2 in a complex with histone H2A peptide== |
| - | <StructureSection load='4edu' size='340' side='right' caption='[[4edu]], [[Resolution|resolution]] 2.58Å' scene=''> | + | <StructureSection load='4edu' size='340' side='right'caption='[[4edu]], [[Resolution|resolution]] 2.58Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4edu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EDU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EDU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4edu]] is a 2 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=4EDU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EDU FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLZ:N-METHYL-LYSINE'>MLZ</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLZ:N-METHYL-LYSINE'>MLZ</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SCML2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4edu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4edu OCA], [https://pdbe.org/4edu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4edu RCSB], [https://www.ebi.ac.uk/pdbsum/4edu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4edu ProSAT]</span></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=4edu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4edu OCA], [http://pdbe.org/4edu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4edu RCSB], [http://www.ebi.ac.uk/pdbsum/4edu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4edu ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SCML2_HUMAN SCML2_HUMAN]] Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development (By similarity). [[http://www.uniprot.org/uniprot/H2AJ_HUMAN H2AJ_HUMAN]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | + | [[https://www.uniprot.org/uniprot/SCML2_HUMAN SCML2_HUMAN]] Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Amaya, M F]] | + | [[Category: Large Structures]] |
| - | [[Category: Arrowsmith, C H]] | + | [[Category: Amaya MF]] |
| - | [[Category: Nady, N]] | + | [[Category: Arrowsmith CH]] |
| - | [[Category: Ravichandran, M]] | + | [[Category: Nady N]] |
| - | [[Category: Tempel, W]] | + | [[Category: Ravichandran M]] |
| - | [[Category: Histone ptm binding]]
| + | [[Category: Tempel W]] |
| - | [[Category: Mbt fold]]
| + | |
| - | [[Category: Methylation]]
| + | |
| - | [[Category: Royal family]]
| + | |
| - | [[Category: Transcription]]
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| Structural highlights
Function
[SCML2_HUMAN] Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development (By similarity).
Publication Abstract from PubMed
Histone methylation has emerged as an important covalent modification involved in a variety of biological processes, especially regulation of transcription and chromatin dynamics. Lysine methylation is found in three distinct states (monomethylation, dimethylation and trimethylation), which are recognized by specific protein domains. The malignant brain tumor (MBT) domain is one such module found in several chromatin regulatory complexes including Polycomb repressive complex 1. Here, we present a comprehensive characterization of the human MBT family with emphasis on histone binding specificity. SPOT-blot peptide arrays were used to screen for the methyllysine-containing histone peptides that bind to MBT domains found in nine human proteins. Selected interactions were quantified using fluorescence polarization assays. We show that all MBT proteins recognize only monomethyllysine and/or dimethyllysine marks and provide evidence that some MBT domains recognize a defined consensus sequence while others bind in a promiscuous, non-sequence-specific manner. Furthermore, using structure-based mutants, we identify a triad of residues in the methyllysine binding pocket that imparts discrimination between monomethyllysine and dimethyllysine. This study represents a comprehensive analysis of MBT substrate specificity, establishing a foundation for the rational design of selective MBT domain inhibitors that may enable elucidation of their role in human biology and disease.
Histone Recognition by Human Malignant Brain Tumor Domains.,Nady N, Krichevsky L, Zhong N, Duan S, Tempel W, Amaya MF, Ravichandran M, Arrowsmith CH J Mol Biol. 2012 Sep 4. pii: S0022-2836(12)00699-7. doi:, 10.1016/j.jmb.2012.08.022. PMID:22954662[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nady N, Krichevsky L, Zhong N, Duan S, Tempel W, Amaya MF, Ravichandran M, Arrowsmith CH. Histone Recognition by Human Malignant Brain Tumor Domains. J Mol Biol. 2012 Sep 4. pii: S0022-2836(12)00699-7. doi:, 10.1016/j.jmb.2012.08.022. PMID:22954662 doi:http://dx.doi.org/10.1016/j.jmb.2012.08.022
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