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A Simple Calixarene Recognizes Post‐translationally Methylated Lysine
Author(s) -
Beshara Cory S.,
Jones Catherine E.,
Daze Kevin D.,
Lilgert Brandin J.,
Hof Fraser
Publication year - 2010
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200900633
Subject(s) - histone , methylation , cationic polymerization , lysine , peptide , chemistry , computational biology , posttranslational modification , biochemistry , residue (chemistry) , gene , combinatorial chemistry , biology , amino acid , enzyme , organic chemistry
Pinning the tail: The post‐translational methylation of proteins governs important biochemical pathways, including many involved in gene regulation and cancer. We report here on the ability of the well known p ‐sulfonatocalix[4]arene to bind strongly to trimethyllysine with good selectivity over all other cationic side chains (see figure), including post‐translationally methylated Arg. We also find that it binds with good site selectively and low μ M affinity to the Lys(Me 3 ) residue on a representative histone tail peptide.