2VYT

The MBT repeats of human SCML2 bind to peptides containing mono methylated lysine.

Summary for 2VYT

• Entry DOI: 10.2210/pdb2vyt/pdb
• Related: 1OI1 2BIV
• Descriptor: SEX COMB ON MIDLEG-LIKE PROTEIN 2, N-METHYL-LYSINE, TRIETHYLENE GLYCOL, ... (4 entities in total)
• Functional Keywords: mono methylated peptides, mbt repeats, transcription, phosphoprotein, alternative splicing, transcription regulation, nucleus, repressor, chromatin, human scml2
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Nucleus : Q9UQR0
• Total number of polymer chains: 2
• Total formula weight: 49772.24

Authors

Santiveri, C.M.,Lechtenberg, B.C.,Allen, M.D.,Sathyamurthy, A.,Jaulent, A.M.,Freund, S.M.V.,Bycroft, M. (deposition date: 2008-07-28, release date: 2008-08-05, Last modification date: 2023-12-13)

Primary citation

Santiveri, C.M.,Lechtenberg, B.C.,Allen, M.D.,Sathyamurthy, A.,Jaulent, A.M.,Freund, S.M.V.,Bycroft, M.
The Malignant Brain Tumor Repeats of Human Scml2 Bind to Peptides Containing Monomethylated Lysine.
J.Mol.Biol., 382:1107-, 2008

PubMed Abstract: 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.

PubMed: 18706910
DOI: 10.1016/J.JMB.2008.07.081

Experimental method

X-RAY DIFFRACTION (1.9 Å)