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''' | '''Crystal Structure of the two MBT repeats from Sex-Comb on Midleg (SCM) in complex with methyl lysine''' | ||
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[[Category: Mueller, C W.]] | [[Category: Mueller, C W.]] | ||
[[Category: Steuerwald, U.]] | [[Category: Steuerwald, U.]] | ||
| - | [[Category: | + | [[Category: Chromatin regulator]] |
| - | [[Category: | + | [[Category: Developmental protein]] |
| - | [[Category: | + | [[Category: Mbt]] |
| - | [[Category: | + | [[Category: Mbt repeat]] |
| - | [[Category: | + | [[Category: Metal-binding]] |
| - | [[Category: | + | [[Category: Nucleus]] |
| - | [[Category: | + | [[Category: Polycomb]] |
| - | [[Category: | + | [[Category: Repressor]] |
| - | [[Category: | + | [[Category: Scm]] |
| - | [[Category: | + | [[Category: Sex comb on midleg]] |
| - | [[Category: | + | [[Category: Transcription]] |
| - | [[Category: | + | [[Category: Transcription regulation]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 16:16:13 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 13:16, 4 May 2008
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. 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 Nov;8(11):1031-7. Epub 2007 Oct 12. PMID:17932512 Page seeded by OCA on Sun May 4 16:16:13 2008
