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Product Summary
Fragment
Residues 171-836<br/>Residues 308-482
Protein Description
Lysine-specific histone demethylase1 complexed with REST corepressor1
Background
Histone modifications, such as acetylation and methylation, are important epigenetic marks that regulate diverse biological processes that use chromatin as the template, including transcription. Dysregulation of histone acetylation and methylation leads to the silencing of tumor suppressor genes and contributes to cancer progression. Inhibitors of enzymes that catalyze the addition and removal of these epigenetic marks thus have therapeutic potential for treating cancer. Lysine-specific demethylase 1 (LSD1) is the first discovered histone lysine demethylase and, with the help of its cofactor CoREST, specifically demethylates mono- and dimethylated histone H3 lysine 4 (H3-K4), thus repressing transcription.
Protein Classification
Oxidoreductase/repressor
Structure Weight
101692.78 Da
PDBID
2UXX
Method
X-Ray Diffraction
Resolution
2.74 Å
Ligand Chemical Component
chloride ion, FA9, glycerol
Reference
Yang, M., Culhane, J.C., Szewczuk, L.M., Jalili, P., Ball, H.L., Machius, M., Cole, P.A., Yu, H.Structural Basis for the Inhibition of the Lsd1 Histone Demethylase by the Antidepressant Trans-2-Phenylcyclopropylamine.Biochemistry, 2007,46: 8058-8065
cDNALength
1998 (LSD1) 705 (CoREST)