4l59

Crystal structure of the 3-MBT repeat domain of L3MBTL3 and UNC2533 complex

spinqualitylabelsall models 4l59, resolution 2.29Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4l59 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.29Å Ligands: 1VZ, SO4, UNX Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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