4l59: Difference between revisions

Line 10:

== Function ==

[[http://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).

== 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>

== References ==

__TOC__

</StructureSection>

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 10: / Line 10: @@
 == Function ==
 [[http://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&reg;/PubMed&reg;, 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>