2uxx

File:2uxx.gif

spinqualitylabelsall models 2uxx, resolution 2.74Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

HUMAN LSD1 HISTONE DEMETHYLASE-COREST IN COMPLEX WITH AN FAD-TRANYLCYPROMINE ADDUCT

OverviewOverview

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. Because LSD1 belongs to the family of flavin adenine, dinucleotide ... [(full description)]

About this StructureAbout this Structure

2UXX is a [Protein complex] structure of sequences from [Homo sapiens] with CL, FA9 and GOL as [ligands]. Full crystallographic information is available from [OCA].

ReferenceReference

Structural basis for the inhibition of the LSD1 histone demethylase by the antidepressant trans-2-phenylcyclopropylamine., Yang M, Culhane JC, Szewczuk LM, Jalili P, Ball HL, Machius M, Cole PA, Yu H, Biochemistry. 2007 Jul 10;46(27):8058-65. Epub 2007 Jun 15. PMID:17569509

Page seeded by OCA on Mon Oct 29 20:21:27 2007