2R5M

Crystal Structure of the two MBT repeats from Sex-Comb on Midleg (SCM) in complex with peptide R-(me)K-S

2R5M の概要

• エントリーDOI: 10.2210/pdb2r5m/pdb
• 関連するPDBエントリー: 2R57 2R58 2R5A
• 分子名称: Polycomb protein Scm, peptide R(me)KS (3 entities in total)
• 機能のキーワード: mbt repeat, polycomb, sex comb on midleg, chromatin regulator, developmental protein, metal-binding, nucleus, repressor, transcription, transcription regulation
• 由来する生物種: Drosophila melanogaster (fruit fly); 詳細
• 細胞内の位置: Nucleus (Probable): Q9VHA0
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 29802.79

構造登録者

Grimm, C.,Steuerwald, U.,Mueller, C.W. (登録日: 2007-09-04, 公開日: 2007-10-30, 最終更新日: 2021-10-20)

主引用文献

Grimm, C.,de Ayala Alonso, A.G.,Rybin, V.,Steuerwald, U.,Ly-Hartig, N.,Fischle, W.,Muller, J.,Muller, C.W.
Structural and functional analyses of methyl-lysine binding by the malignant brain tumour repeat protein Sex comb on midleg.
Embo Rep., 8:1031-1037, 2007

PubMed 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.

PubMed: 17932512
DOI: 10.1038/sj.embor.7401085

実験手法

X-RAY DIFFRACTION (2.65 Å)