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| [[Image:2v1d.jpg|left|200px]] | | {{Seed}} |
| | [[Image:2v1d.png|left|200px]] |
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| {{STRUCTURE_2v1d| PDB=2v1d | SCENE= }} | | {{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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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17537733}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17537733 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17537733}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Transcription]] | | [[Category: Transcription]] |
| [[Category: Transcription regulation]] | | [[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 Tue Jul 29 09:28:34 2008'' |
