2v1d

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|PDB= 2v1d |SIZE=350|CAPTION= <scene name='initialview01'>2v1d</scene>, resolution 3.10&Aring;
|PDB= 2v1d |SIZE=350|CAPTION= <scene name='initialview01'>2v1d</scene>, resolution 3.10&Aring;
|SITE= <scene name='pdbsite=AC1:Fad+Binding+Site+For+Chain+A'>AC1</scene>
|SITE= <scene name='pdbsite=AC1:Fad+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene>
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|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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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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}}
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[[Category: Forneris, F.]]
[[Category: Forneris, F.]]
[[Category: Mattevi, A.]]
[[Category: Mattevi, A.]]
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[[Category: FAD]]
 
[[Category: alternative splicing]]
[[Category: alternative splicing]]
[[Category: amine oxidase]]
[[Category: amine oxidase]]
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[[Category: transcription regulation]]
[[Category: transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:42:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:07:24 2008''

Revision as of 02:07, 31 March 2008

Image:2v1d.jpg


PDB ID 2v1d

Drag the structure with the mouse to rotate
, resolution 3.10Å
Sites:
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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