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| {{STRUCTURE_2hko| PDB=2hko | SCENE= }} | | {{STRUCTURE_2hko| PDB=2hko | SCENE= }} |
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| '''Crystal structure of LSD1'''
| | ===Crystal structure of LSD1=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16956976}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16956976 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16956976}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Fad binding domain]] | | [[Category: Fad binding domain]] |
| [[Category: Swirm domain]] | | [[Category: Swirm domain]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:24:10 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:27:17 2008'' |
