2hko
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Crystal structure of LSD1
OverviewOverview
Lysine-specific demethylase 1 (LSD1) was recently identified as the first, histone demethylase that specifically demethylates monomethylated and, dimethylated histone H3 at K4. It is a component of the CoREST and other, corepressor complexes and plays an important role in silencing, neuronal-specific genes in nonneuronal cells, but the molecular mechanisms, of its action remain unclear. The 2.8-A-resolution crystal structure of, the human LSD1 reveals that LSD1 defines a new subfamily of FAD-dependent, oxidases. The active center of LSD1 is characterized by a remarkable, 1,245-A3 substrate-binding cavity with a highly negative electrostatic, potential. Although the protein core of LSD1 resembles other flavoenzymes, its enzymatic activity and functions require two additional structural, modules: an N-terminal SWIRM domain important for protein stability and a, large insertion in the catalytic domain indispensable both for the, demethylase activity and the interaction with CoREST. These results, provide a framework for further probing the catalytic mechanism and the, functional roles of LSD1.
About this StructureAbout this Structure
2HKO is a Single protein structure of sequence from Homo sapiens with FAD as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of human histone lysine-specific demethylase 1 (LSD1)., Chen Y, Yang Y, Wang F, Wan K, Yamane K, Zhang Y, Lei M, Proc Natl Acad Sci U S A. 2006 Sep 19;103(38):13956-61. Epub 2006 Sep 6. PMID:16956976
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