2r5a
From Proteopedia
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Crystal Structure of the two MBT repeats from Sex-Comb on Midleg (SCM) in complex with methyl lysine
Overview
Sex comb on midleg (Scm) is a member of the Polycomb group of proteins, involved in the maintenance of repression of Hox and other developmental, control genes in Drosophila. The two malignant brain tumour (MBT) repeats, of Scm form a domain that preferentially binds to monomethylated lysine, residues either as a free amino acid or in the context of peptides, while, unmodified or di- or trimethylated lysine residues are bound with, significantly lower affinity. The crystal structure of a, monomethyl-lysine-containing histone tail peptide bound to the MBT repeat, domain shows that the methyl-lysine side chain occupies a binding pocket, in the second MBT repeat formed by three conserved aromatic residues and, one aspartate. Insertion of the monomethylated side chain into this pocket, seems to be the main contributor to the binding affinity. Functional, analyses in Drosophila show that the MBT domain of Scm and its, methyl-lysine-binding activity are required for repression of Hox genes.
About this Structure
2R5A is a Single protein structure of sequence from Drosophila melanogaster with as ligand. Full crystallographic information is available from OCA.
Reference
Structural and functional analyses of methyl-lysine binding by the malignant brain tumour repeat protein Sex comb on midleg., Grimm C, de Ayala Alonso AG, Rybin V, Steuerwald U, Ly-Hartig N, Fischle W, Muller J, Muller CW, EMBO Rep. 2007 Oct 12;. PMID:17932512
Page seeded by OCA on Wed Jan 23 12:38:19 2008
