Crystal structure of human histone lysine-specific demethylase 1 (LSD1).

Crystal structure of human histone lysine-specific demethylase 1 (LSD1). Research Abstract Details 

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Crystal structure of human histone lysine-specific demethylase 1 (LSD1). Abstract Text:

Yong Chen,Yuting Yang,Feng Wang,Ke Wan,Kenichi Yamane,Yi Zhang,Ming Lei,

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.

Crystal structure of human histone lysine-specific demethylase 1 (LSD1). Publishing Authors By Initials

Y Chen,Y Yang,F Wang,K Wan,K Yamane,Y Zhang,M Lei,

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Crystal structure of human histone lysine-specific demethylase 1 (LSD1). Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Proceedings of the National Academy of Sciences of

VOLUME: 103

Page Numbers: 13956-61

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ISSN: 0027-8424

DAY: 6

MONTH: 09

YEAR: 2006

Crystal structure of human histone lysine-specific demethylase 1 (LSD1). Information

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LANGUAGE: eng

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Grant and Affiliation Information for Crystal structure of human histone lysine-specific demethylase 1 (LSD1).

AFFILIATION: Department of Biological Chemistry, University of Michigan Medical School, 5413 Medical Science I, 1301 Catherine Road, Ann Arbor, MI 48109-0606, USA.

Country: United States

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MEDLINETA: Proc Natl Acad Sci U S A

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