The recognition specificity of the CHD1 chromodomain with modified histone H3 peptides.

ABSTRACT: Histone tail peptides comprise the flexible portion of chromatin, the substance which serves as the packaging for the eukaryotic genome. According to the histone code hypothesis, reader protein domains (chromodomains) can recognize modifications of amino acid residues within these peptides, regulating the expression of genes. We have performed simulations on models of chromodomain helicase DNA-binding protein 1 complexed with a variety of histone H3 modifications. Binding free energies for both the overall complexes and the individual residues within the protein and peptides were computed with molecular mechanics-generalized Born surface area. The simulation results agree well with experimental data and identify several chromodomain helicase DNA-binding protein 1 residues that play key rol

SUBMITTER: Stein RS 

PROVIDER: S-EPMC3034827 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature