Lysine-specific histone demethylase
From Proteopedia
Lysine-specific histone demethylase 1 (LSD1) is a flavin-dependent oxidase that catalyzes the removal of methyl groups from mono- and dimethylated lysine 4 of histone H3. LSD1 is a nuclear homolog of amine oxidase. It functions as histone demethylase and transcriptional corepressor. LSD1 demethylation occurs via a reaction which produces formaldehyde. LSD1 is a component of transcriptional corepressor complex which also contains CoREST (corepressor of element-1-silencing transcription factor).
3D structures of lysine-specific histone demethylase 1
2com, 2l3d - hLSD1 SWIRM domain – human – NMR
2h94, 2dw4, 2z3y, 2z5u – hLSD1
2hko – hLSD1 (mutant)
2ejr, 3abt, 3abu – hLSD1 + tranylcypromine derivative
LSD1 complex with CoREST
2iw5, 2uxn, 2uxx - hLSD1 SWIRM + amine oxidase domains + CoREST SANT1 and SANT2 domains
2v1d - hLSD1 residues 123-852 + CoREST SANT1 and SANT2 domains + histone H3 residues 2-22 (mutant)
2x0l - hLSD1 residues 123-852 + CoREST SANT1 and SANT2 domains + histone H3 residues 1-16
2xaf, 2xag, 2xah, 2xaj, 2xaq, 2xas - hLSD1 residues 123-852 + CoREST SANT1 and SANT2 domains + tranylcypromine derivative
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Joel L. Sussman, Jaime Prilusky
