2czy

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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

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