Structural highlights
Function
[LMBL2_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. Its association with a chromatin-remodeling complex suggests that it may contribute to prevent expression of genes that trigger the cell into mitosis. Binds to monomethylated and dimethylated 'Lys-20' on histone H4. Binds histone H3 peptides that are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27'.[1]
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
Polycomb group proteins are epigenetic regulators that maintain patterns of gene expression over multiple rounds of cell division. Many of these proteins, including polyhomeotic and the MBT repeat containing proteins SCM and dSfmbt, contain an atypical C2C2 zinc finger with a characteristic phenylalanine-cysteine-serine sequence motif. The reoccurrence of this so-called FCS zinc finger in a variety of polycomb group proteins suggests that it has an important regulatory function. We have determined the solution structure of the FCS zinc finger of the human dSfmbt homologue L(3)mbt-like 2 (L3MBTL2). The structure consists of a beta-hairpin followed by an alpha-helix. The zinc ligands are situated in the beta-hairpin and at the N-terminus of the alpha-helix an arrangement typical of the treble clef class of zinc fingers. The structure is consistent with the proposal that FCS zinc fingers bind to regulatory RNAs.
Solution structure of the FCS zinc finger domain of the human polycomb group protein L(3)mbt-like 2.,Lechtenberg BC, Allen MD, Rutherford TJ, Freund SM, Bycroft M Protein Sci. 2009 Mar;18(3):657-61. PMID:19241375[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Guo Y, Nady N, Qi C, Allali-Hassani A, Zhu H, Pan P, Adams-Cioaba MA, Amaya MF, Dong A, Vedadi M, Schapira M, Read RJ, Arrowsmith CH, Min J. Methylation-state-specific recognition of histones by the MBT repeat protein L3MBTL2. Nucleic Acids Res. 2009 Apr;37(7):2204-10. Epub 2009 Feb 20. PMID:19233876 doi:10.1093/nar/gkp086
- ↑ Lechtenberg BC, Allen MD, Rutherford TJ, Freund SM, Bycroft M. Solution structure of the FCS zinc finger domain of the human polycomb group protein L(3)mbt-like 2. Protein Sci. 2009 Mar;18(3):657-61. PMID:19241375 doi:10.1002/pro.51
