2iw5
From Proteopedia
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==Overview== | ==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, .. | + | 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== | ==About this Structure== | ||
| - | 2IW5 is a | + | 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]. Structure known Active Site: AC1. 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 Mon Nov 5 13:23:25 2007'' |
Revision as of 11:18, 5 November 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. Structure known Active 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
Page seeded by OCA on Mon Nov 5 13:23:25 2007
Categories: 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
