2R5M: Crystal Structure Of The Two Mbt Repeats From Sex-Comb On Midleg (Scm) In Complex With Peptide R-(Me)k-S

Citation:
Abstract
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.
PDB ID: 2R5MDownload
MMDB ID: 60291
PDB Deposition Date: 2007/9/4
Updated in MMDB: 2007/11
Experimental Method:
x-ray diffraction
Resolution: 2.65  Å
Source Organism:
synthetic construct
Similar Structures:
Biological Unit for 2R5M: dimeric; determined by author and by software (PISA)
Molecular Components in 2R5M
Label Count Molecule
Proteins (2 molecules)
1
Polycomb Protein SCM(Gene symbol: Scm)
Molecule annotation
1
Peptide R(me)ks
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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