2biv

Crystal structure of the wild-type MBT domains of Human SCML2

spinqualitylabelsall models 2biv, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2biv is a 3 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 1.7Å Ligands: IOD, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed SCML2 (sex comb on midleg-like 2) is a constituent of the Polycomb repressive complex 1, a large multiprotein assembly required for the repression of developmental control genes. It contains two MBT (malignant brain tumor) repeats; the MBT is a protein module structurally similar to domains that bind to methylated histones. We have used NMR spectroscopy to examine the binding specificity of these repeats. Our data show that they preferentially bind histone peptides monomethylated at lysine residues with no apparent sequence specificity. The crystal structure of the complex between the protein and monomethyllysine reveals that the modified amino acid binds to an aromatic rich pocket at one end of the beta-barrel of the second repeat. The malignant brain tumor repeats of human SCML2 bind to peptides containing monomethylated lysine.,Santiveri CM, Lechtenberg BC, Allen MD, Sathyamurthy A, Jaulent AM, Freund SM, Bycroft M J Mol Biol. 2008 Oct 24;382(5):1107-12. Epub 2008 Aug 3. PMID:18706910 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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