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2v1d
From Proteopedia
| 2v1d, resolution 3.10Å () | |||||||||
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| Related: | 2x0l, 2uxx, 2iw5, 2uxn, 2com, 2h94 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
STRUCTURAL BASIS OF LSD1-COREST SELECTIVITY IN HISTONE H3 RECOGNITION
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 oxidation of the substrate amino-methyl group. These features dictate the exquisite substrate specificity of LSD1 and provide a structural framework to explain the fine tuning of its catalytic activity and the active role of CoREST in substrate recognition.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
2V1D is a 3 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Forneris F, Binda C, Adamo A, Battaglioli E, Mattevi A. Structural basis of LSD1-CoREST selectivity in histone H3 recognition. J Biol Chem. 2007 Jul 13;282(28):20070-4. Epub 2007 May 30. PMID:17537733 doi:10.1074/jbc.C700100200
Page seeded by OCA on Wed Dec 30 14:53:03 2009
Categories: Homo sapiens | Adamo, A. | Battaglioli, E. | Binda, C. | Forneris, F. | Mattevi, A. | Alternative splicing | Chromatin regulator | Chromatin remodelling | Flavin | Host-virus interaction | Nuclear protein | Oxidoreductase | Oxidoreductase repressor complex | Phosphorylation | Repressor | Transcription regulation
