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2v1d

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[[Image:2v1d.jpg|left|200px]]
[[Image:2v1d.jpg|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_2v1d", creates the "Structure Box" on the page.
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{{STRUCTURE_2v1d| PDB=2v1d | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v1d OCA], [http://www.ebi.ac.uk/pdbsum/2v1d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2v1d RCSB]</span>
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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.]]
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[[Category: alternative splicing]]
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[[Category: Alternative splicing]]
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[[Category: amine oxidase]]
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[[Category: Amine oxidase]]
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[[Category: chromatin regulator]]
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[[Category: Chromatin regulator]]
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[[Category: coiled coil]]
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[[Category: Coiled coil]]
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[[Category: fad]]
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[[Category: Fad]]
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[[Category: flavin]]
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[[Category: Flavin]]
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[[Category: histone demethylase]]
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[[Category: Histone demethylase]]
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[[Category: host-virus interaction]]
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[[Category: Host-virus interaction]]
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[[Category: lsd1]]
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[[Category: Lsd1]]
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[[Category: nuclear protein]]
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[[Category: Nuclear protein]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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[[Category: oxidoreductase/repressor complex chromatin remodelling]]
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[[Category: Oxidoreductase/repressor complex chromatin remodelling]]
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[[Category: phosphorylation]]
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[[Category: Phosphorylation]]
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[[Category: repressor]]
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[[Category: Repressor]]
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[[Category: transcription]]
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[[Category: Transcription]]
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[[Category: transcription regulation]]
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[[Category: Transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:01:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:07:24 2008''
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Revision as of 15:01, 4 May 2008

Template:STRUCTURE 2v1d

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

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