Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2007-11-1
pubmed:abstractText
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:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/17932512-11222153, http://linkedlifedata.com/resource/pubmed/commentcorrection/17932512-11859155, http://linkedlifedata.com/resource/pubmed/commentcorrection/17932512-12575993, http://linkedlifedata.com/resource/pubmed/commentcorrection/17932512-12842041, http://linkedlifedata.com/resource/pubmed/commentcorrection/17932512-12952983, http://linkedlifedata.com/resource/pubmed/commentcorrection/17932512-1350533, http://linkedlifedata.com/resource/pubmed/commentcorrection/17932512-15299374, http://linkedlifedata.com/resource/pubmed/commentcorrection/17932512-16415788, http://linkedlifedata.com/resource/pubmed/commentcorrection/17932512-16601153, http://linkedlifedata.com/resource/pubmed/commentcorrection/17932512-16618800, http://linkedlifedata.com/resource/pubmed/commentcorrection/17932512-16728977, http://linkedlifedata.com/resource/pubmed/commentcorrection/17932512-16914306, http://linkedlifedata.com/resource/pubmed/commentcorrection/17932512-17043307, http://linkedlifedata.com/resource/pubmed/commentcorrection/17932512-17173055, http://linkedlifedata.com/resource/pubmed/commentcorrection/17932512-3098596, http://linkedlifedata.com/resource/pubmed/commentcorrection/17932512-8625848, http://linkedlifedata.com/resource/pubmed/commentcorrection/17932512-9755199
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1469-221X
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1031-7
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:17932512-Amino Acid Sequence, pubmed-meshheading:17932512-Animals, pubmed-meshheading:17932512-Crystallography, X-Ray, pubmed-meshheading:17932512-DNA-Binding Proteins, pubmed-meshheading:17932512-Drosophila Proteins, pubmed-meshheading:17932512-Drosophila melanogaster, pubmed-meshheading:17932512-Gene Expression Regulation, Developmental, pubmed-meshheading:17932512-Genes, Homeobox, pubmed-meshheading:17932512-Histones, pubmed-meshheading:17932512-Lysine, pubmed-meshheading:17932512-Methylation, pubmed-meshheading:17932512-Models, Molecular, pubmed-meshheading:17932512-Molecular Sequence Data, pubmed-meshheading:17932512-Peptides, pubmed-meshheading:17932512-Protein Conformation, pubmed-meshheading:17932512-Protein Structure, Tertiary, pubmed-meshheading:17932512-Repressor Proteins, pubmed-meshheading:17932512-Sequence Alignment, pubmed-meshheading:17932512-Transgenes
pubmed:year
2007
pubmed:articleTitle
Structural and functional analyses of methyl-lysine binding by the malignant brain tumour repeat protein Sex comb on midleg.
pubmed:affiliation
European Molecular Biology Laboratory, Grenoble Outstation, 6 Rue Jules Horowitz, 38042 Grenoble, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't