2iw5

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|PDB= 2iw5 |SIZE=350|CAPTION= <scene name='initialview01'>2iw5</scene>, resolution 2.57&Aring;
|PDB= 2iw5 |SIZE=350|CAPTION= <scene name='initialview01'>2iw5</scene>, resolution 2.57&Aring;
|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene>
|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</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=2iw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iw5 OCA], [http://www.ebi.ac.uk/pdbsum/2iw5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2iw5 RCSB]</span>
}}
}}
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[[Category: Yang, M.]]
[[Category: Yang, M.]]
[[Category: Yu, H.]]
[[Category: Yu, H.]]
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[[Category: CL]]
 
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[[Category: FAD]]
 
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[[Category: GOL]]
 
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[[Category: NH4]]
 
[[Category: alternative splicing]]
[[Category: alternative splicing]]
[[Category: chromatin demethylation]]
[[Category: chromatin demethylation]]
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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 17:34:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:49:27 2008''

Revision as of 00:49, 31 March 2008

Image:2iw5.gif


PDB ID 2iw5

Drag the structure with the mouse to rotate
, resolution 2.57Å
Sites:
Ligands: , , ,
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



STRUCTURAL BASIS FOR COREST-DEPENDENT DEMETHYLATION OF NUCLEOSOMES BY THE HUMAN LSD1 HISTONE DEMETHYLASE


Overview

Histone methylation regulates diverse chromatin-templated processes, including transcription. Many transcriptional corepressor complexes contain lysine-specific demethylase 1 (LSD1) and CoREST that collaborate to demethylate mono- and dimethylated H3-K4 of nucleosomes. Here, we report the crystal structure of the LSD1-CoREST complex. LSD1-CoREST forms an elongated structure with a long stalk connecting the catalytic domain of LSD1 and the CoREST SANT2 domain. LSD1 recognizes a large segment of the H3 tail through a deep, negatively charged pocket at the active site and possibly a shallow groove on its surface. CoREST SANT2 interacts with DNA. Disruption of the SANT2-DNA interaction diminishes CoREST-dependent demethylation of nucleosomes by LSD1. The shape and dimension of LSD1-CoREST suggest its bivalent binding to nucleosomes, allowing efficient H3-K4 demethylation. This spatially separated, multivalent nucleosome binding mode may apply to other chromatin-modifying enzymes that generally contain multiple nucleosome binding modules.

About this Structure

2IW5 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis for CoREST-dependent demethylation of nucleosomes by the human LSD1 histone demethylase., Yang M, Gocke CB, Luo X, Borek D, Tomchick DR, Machius M, Otwinowski Z, Yu H, Mol Cell. 2006 Aug 4;23(3):377-87. PMID:16885027

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