2v1d | pdb_00002v1d

STRUCTURAL BASIS OF LSD1-COREST SELECTIVITY IN HISTONE H3 RECOGNITION

File:2v1d.gif

spinqualitylabelsall models 2v1d, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D

Overview

Histone demethylase LSD1 regulates transcription by demethylating Lys(4), of histone H3. The crystal structure of the enzyme in complex with CoREST, and a substrate-like peptide inhibitor highlights an intricate network of, interactions and a folded conformation of the bound peptide. The core of, the peptide structure is formed by Arg(2), Gln(5), and Ser(10), which are, engaged in specific intramolecular H-bonds. Several charged side chains on, the surface of the substrate-binding pocket establish electrostatic, interactions with the peptide. The three-dimensional structure predicts, that methylated Lys(4) binds in a solvent inaccessible position in front, of the flavin cofactor. This geometry is fully consistent with the, demethylation reaction being catalyzed through a flavin-mediated ... [(full description)]

About this Structure

2V1D is a [Protein complex] structure of sequences from [Homo sapiens] with FAD as [ligand]. Full crystallographic information is available from [OCA].

Reference

Structural Basis of LSD1-CoREST Selectivity in Histone H3 Recognition., Forneris F, Binda C, Adamo A, Battaglioli E, Mattevi A, J Biol Chem. 2007 Jul 13;282(28):20070-4. Epub 2007 May 30. PMID:17537733

Page seeded by OCA on Mon Oct 29 19:30:45 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA