Ontology highlight
ABSTRACT:
SUBMITTER: Baron R
PROVIDER: S-EPMC3059804 | biostudies-literature | 2011 Feb
REPOSITORIES: biostudies-literature
Baron Riccardo R Binda Claudia C Tortorici Marcello M McCammon J Andrew JA Mattevi Andrea A
Structure (London, England : 1993) 20110201 2
Histone demethylases LSD1 and LSD2 (KDM1A/B) catalyze the oxidative demethylation of Lys4 of histone H3. We used molecular dynamics simulations to probe the diffusion of the oxygen substrate. Oxygen can reach the catalytic center independently from the presence of a bound histone peptide, implying that LSD1 can complete subsequent demethylation cycles without detaching from the nucleosomal particle. The simulations highlight the role of a strictly conserved active-site Lys residue providing gene ...[more]