2czy
From Proteopedia
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[[Image:2czy.gif|left|200px]] | [[Image:2czy.gif|left|200px]] | ||
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'''Solution structure of the NRSF/REST-mSin3B PAH1 complex''' | '''Solution structure of the NRSF/REST-mSin3B PAH1 complex''' | ||
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[[Category: Nomura, M.]] | [[Category: Nomura, M.]] | ||
[[Category: Uda-Tochio, H.]] | [[Category: Uda-Tochio, H.]] | ||
| - | [[Category: | + | [[Category: Nrsf]] |
| - | [[Category: | + | [[Category: Pah1]] |
| - | [[Category: | + | [[Category: Sin3]] |
| - | [[Category: | + | [[Category: Transcriptional repressor]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 23:26:34 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 20:26, 3 May 2008
Solution structure of the NRSF/REST-mSin3B PAH1 complex
Overview
In non-neuronal cells and neuronal progenitors, many neuron-specific genes are repressed by a neural restrictive silencer factor (NRSF)/repressor element 1 silencing transcription factor (REST), which is an essential transcriptional repressor recruiting the Sin3-HDAC complex. Sin3 contains four paired amphipathic helix (PAH) domains, PAH1, PAH2, PAH3 and PAH4. A specific target repressor for Sin3 is likely to bind to one of them independently. So far, only the tertiary structures of PAH2 domain complexes, when bound to the Sin3-interacting domains of Mad1 and HBP1, have been determined. Here, we reveal that the N-terminal repressor domain of NRSF/REST binds to the PAH1 domain of mSin3B, and determine the structure of the PAH1 domain associated with the NRSF/REST minimal repressor domain. Compared to the PAH2 structure, PAH1 holds a rather globular four-helix bundle structure with a semi-ordered C-terminal tail. In contrast to the amphipathic alpha-helix of Mad1 or HBP1 bound to PAH2, the short hydrophobic alpha-helix of NRSF/REST is captured in the cleft of PAH1. A nuclear hormone receptor corepressor, N-CoR has been found to bind to the PAH1 domain with a lower affinity than NRSF/REST by using its C-terminal region, which contains fewer hydrophobic amino acid residues than the NRSF/REST helix. For strong binding to a repressor, PAH1 seems to require a short alpha-helix consisting of mostly hydrophobic amino acid residues within the repressor. Each of the four PAH domains of Sin3 seems to interact with a characteristic helix of a specific repressor; PAH1 needs a mostly hydrophobic helix and PAH2 needs an amphipathic helix in each target repressor.
About this Structure
2CZY is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
The neural repressor NRSF/REST binds the PAH1 domain of the Sin3 corepressor by using its distinct short hydrophobic helix., Nomura M, Uda-Tochio H, Murai K, Mori N, Nishimura Y, J Mol Biol. 2005 Dec 9;354(4):903-15. Epub 2005 Oct 26. PMID:16288918 Page seeded by OCA on Sat May 3 23:26:34 2008
Categories: Mus musculus | Protein complex | Mori, N. | Murai, K. | Nishimura, Y. | Nomura, M. | Uda-Tochio, H. | Nrsf | Pah1 | Sin3 | Transcriptional repressor
