2iw5: Difference between revisions
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[[Image:2iw5.gif|left|200px]]<br /> | [[Image:2iw5.gif|left|200px]]<br /><applet load="2iw5" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="2iw5" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="2iw5, resolution 2.57Å" /> | caption="2iw5, resolution 2.57Å" /> | ||
'''STRUCTURAL BASIS FOR COREST-DEPENDENT DEMETHYLATION OF NUCLEOSOMES BY THE HUMAN LSD1 HISTONE DEMETHYLASE'''<br /> | '''STRUCTURAL BASIS FOR COREST-DEPENDENT DEMETHYLATION OF NUCLEOSOMES BY THE HUMAN LSD1 HISTONE DEMETHYLASE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2IW5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CL, NH4, FAD and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. | 2IW5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CL, NH4, FAD and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Gol Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IW5 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 19:37:23 2007'' | ||
Revision as of 17:27, 18 December 2007
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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 with CL, NH4, FAD and GOL as ligands. Known structural/functional Site: AC1. 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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Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- Homo sapiens
- Protein complex
- Borek, D.
- Gocke, C.B.
- Luo, X.
- Machius, M.
- Otwinowski, Z.
- Tomchick, D.R.
- Yang, M.
- Yu, H.
- CL
- FAD
- GOL
- NH4
- Alternative splicing
- Chromatin demethylation
- Chromatin regulator
- Coiled coil
- Corest
- Fad
- Histone demethylase
- Host-virus interaction
- Lsd1
- Nuclear protein
- Nucleosomes
- Oxidoreductase
- Oxidoreductase/repressor complex
- Phosphorylation
- Repressor
- Transcription
- Transcription regulation