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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
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- 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
