4l59: Difference between revisions
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== | ==Crystal structure of the 3-MBT repeat domain of L3MBTL3 and UNC2533 complex== | ||
[[http://www.uniprot.org/uniprot/LMBL3_HUMAN LMBL3_HUMAN | <StructureSection load='4l59' size='340' side='right'caption='[[4l59]], [[Resolution|resolution]] 2.29Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4l59]] 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=4L59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L59 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.29Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1VZ:4-(PYRROLIDIN-1-YL)-1-{4-[2-(PYRROLIDIN-1-YL)ETHYL]PHENYL}PIPERIDINE'>1VZ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</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=4l59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l59 OCA], [https://pdbe.org/4l59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l59 RCSB], [https://www.ebi.ac.uk/pdbsum/4l59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l59 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/LMBL3_HUMAN LMBL3_HUMAN] Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility. Required for normal maturation of myeloid progenitor cells (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We recently reported the discovery of UNC1215, a potent and selective chemical probe for the L3MBTL3 methyllysine reader domain. In this article, we describe the development of structure-activity relationships (SAR) of a second series of potent L3MBTL3 antagonists which evolved from the structure of the chemical probe UNC1215. These compounds are selective for L3MBTL3 against a panel of methyllysine reader proteins, particularly the related MBT family proteins, L3MBTL1 and MBTD1. A co-crystal structure of L3MBTL3 and one of the most potent compounds suggests that the L3MBTL3 dimer rotates about the dimer interface to accommodate ligand binding. | |||
The structure-activity relationships of L3MBTL3 inhibitors: flexibility of the dimer interface.,Camerino MA, Zhong N, Dong A, Dickson BM, James LI, Baughman BM, Norris JL, Kireev DB, Janzen WP, Arrowsmith CH, Frye SV Medchemcomm. 2013 Nov;4(11):1501-1507. doi: 10.1039/C3MD00197K. PMID:24466405<ref>PMID:24466405</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4l59" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Arrowsmith | [[Category: Large Structures]] | ||
[[Category: | [[Category: Arrowsmith CH]] | ||
[[Category: | [[Category: Baughman BM]] | ||
[[Category: | [[Category: Bountra C]] | ||
[[Category: | [[Category: Brown PJ]] | ||
[[Category: | [[Category: Camerino MA]] | ||
[[Category: | [[Category: Dickson BM]] | ||
[[Category: | [[Category: Dong A]] | ||
[[Category: | [[Category: Edwards AM]] | ||
[[Category: | [[Category: Frye SV]] | ||
[[Category: | [[Category: Graslund S]] | ||
[[Category: | [[Category: James LI]] | ||
[[Category: | [[Category: Janzen WP]] | ||
[[Category: | [[Category: Kireev DB]] | ||
[[Category: | [[Category: Norris JL]] | ||
[[Category: | [[Category: Ravichandran M]] | ||
[[Category: Zhong N]] | |||
Latest revision as of 19:11, 20 September 2023
Crystal structure of the 3-MBT repeat domain of L3MBTL3 and UNC2533 complexCrystal structure of the 3-MBT repeat domain of L3MBTL3 and UNC2533 complex
Structural highlights
FunctionLMBL3_HUMAN Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility. Required for normal maturation of myeloid progenitor cells (By similarity). Publication Abstract from PubMedWe recently reported the discovery of UNC1215, a potent and selective chemical probe for the L3MBTL3 methyllysine reader domain. In this article, we describe the development of structure-activity relationships (SAR) of a second series of potent L3MBTL3 antagonists which evolved from the structure of the chemical probe UNC1215. These compounds are selective for L3MBTL3 against a panel of methyllysine reader proteins, particularly the related MBT family proteins, L3MBTL1 and MBTD1. A co-crystal structure of L3MBTL3 and one of the most potent compounds suggests that the L3MBTL3 dimer rotates about the dimer interface to accommodate ligand binding. The structure-activity relationships of L3MBTL3 inhibitors: flexibility of the dimer interface.,Camerino MA, Zhong N, Dong A, Dickson BM, James LI, Baughman BM, Norris JL, Kireev DB, Janzen WP, Arrowsmith CH, Frye SV Medchemcomm. 2013 Nov;4(11):1501-1507. doi: 10.1039/C3MD00197K. PMID:24466405[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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