2v1d
From Proteopedia
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| - | + | {{STRUCTURE_2v1d| PDB=2v1d | SCENE= }} | |
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'''STRUCTURAL BASIS OF LSD1-COREST SELECTIVITY IN HISTONE H3 RECOGNITION''' | '''STRUCTURAL BASIS OF LSD1-COREST SELECTIVITY IN HISTONE H3 RECOGNITION''' | ||
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[[Category: Forneris, F.]] | [[Category: Forneris, F.]] | ||
[[Category: Mattevi, A.]] | [[Category: Mattevi, A.]] | ||
| - | [[Category: | + | [[Category: Alternative splicing]] |
| - | [[Category: | + | [[Category: Amine oxidase]] |
| - | [[Category: | + | [[Category: Chromatin regulator]] |
| - | [[Category: | + | [[Category: Coiled coil]] |
| - | [[Category: | + | [[Category: Fad]] |
| - | [[Category: | + | [[Category: Flavin]] |
| - | [[Category: | + | [[Category: Histone demethylase]] |
| - | [[Category: | + | [[Category: Host-virus interaction]] |
| - | [[Category: | + | [[Category: Lsd1]] |
| - | [[Category: | + | [[Category: Nuclear protein]] |
| - | [[Category: | + | [[Category: Oxidoreductase]] |
| - | [[Category: | + | [[Category: Oxidoreductase/repressor complex chromatin remodelling]] |
| - | [[Category: | + | [[Category: Phosphorylation]] |
| - | [[Category: | + | [[Category: Repressor]] |
| - | [[Category: | + | [[Category: Transcription]] |
| - | [[Category: | + | [[Category: Transcription regulation]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:01:43 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 15:01, 4 May 2008
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. 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 Sun May 4 18:01:43 2008
Categories: Homo sapiens | Protein complex | Adamo, A. | Battaglioli, E. | Binda, C. | Forneris, F. | Mattevi, A. | 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
