View source for 7mbm


==Cryo-EM structure of MLL1-NCP (H3K4M) complex, mode01==
<StructureSection load='7mbm' size='340' side='right'caption='[[7mbm]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7mbm]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] 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=7MBM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MBM FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy</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=7mbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mbm OCA], [https://pdbe.org/7mbm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mbm RCSB], [https://www.ebi.ac.uk/pdbsum/7mbm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mbm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RBBP5_HUMAN RBBP5_HUMAN] In embryonic stem (ES) cells, plays a crucial role in the differentiation potential, particularly along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci, including that mediated by retinoic acid (By similarity). As part of the MLL1/MLL complex, involved in mono-, di- and trimethylation at 'Lys-4' of histone H3. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation.<ref>PMID:19556245</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cryo-EM structures of the KMT2A/MLL1 core complex bound on nucleosome core particles (NCPs) suggest unusual rotational dynamics of the MLL1 complex approaching its physiological substrate. However, the functional implication of such dynamics remains unclear. Here, we show that the MLL1 core complex also shows high rotational dynamics bound on the NCP carrying the catalytically inert histone H3 lysine 4 to methionine (K4M) mutation. There are two major binding modes of the MLL1 complex on the NCP(K4M). Importantly, disruption of only one of the binding modes compromised the overall MLL1 activity in an NCP-specific manner. We propose that the MLL1 core complex probably exists in an equilibrium of poised and active binding modes. The high rotational dynamics of the MLL1 complex on the NCP is a feature that can be exploited for loci-specific regulation of H3K4 methylation in higher eukaryotes.

Regulation of MLL1 Methyltransferase Activity in Two Distinct Nucleosome Binding Modes.,Ayoub A, Park SH, Lee YT, Cho US, Dou Y Biochemistry. 2022 Jan 4;61(1):1-9. doi: 10.1021/acs.biochem.1c00603. Epub 2021 , Dec 20. PMID:34928138<ref>PMID:34928138</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7mbm" style="background-color:#fffaf0;"></div>

==See Also==
*[[Histone 3D structures|Histone 3D structures]]
*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
*[[Retinoblastoma-binding protein 3D structures|Retinoblastoma-binding protein 3D structures]]
*[[WD-repeat protein 3D structures|WD-repeat protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Xenopus laevis]]
[[Category: Ayoub A]]
[[Category: Cho U]]
[[Category: Dou Y]]
[[Category: Lee YT]]
[[Category: Park SH]]