2v1d
From Proteopedia
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==Overview== | ==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 .. | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 2V1D is a | + | 2V1D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with FAD as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2V1D OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:06:49 2007'' |
Revision as of 12:01, 5 November 2007
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STRUCTURAL BASIS OF LSD1-COREST SELECTIVITY IN HISTONE H3 RECOGNITION
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 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.
About this Structure
2V1D is a Protein complex structure of sequences from Homo sapiens with FAD as ligand. Structure known Active Site: AC1. 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 Nov 5 14:06:49 2007
Categories: Homo sapiens | Protein complex | Adamo, A. | Battaglioli, E. | Binda, C. | Forneris, F. | Mattevi, A. | FAD | Alternative splicing | Amine oxidase | Chromatin regulator | Coiled coil | Fad | Flavin | Histone demethylase | Host-virus interaction | Lsd1 | Nuclear protein | Oxidoreductase | Oxidoreductase/repressor complex chromatin remodelling | Phosphorylation | Repressor | Transcription | Transcription regulation
