2CZY

Solution structure of the NRSF/REST-mSin3B PAH1 complex

2CZY の概要

• エントリーDOI: 10.2210/pdb2czy/pdb
• NMR情報: BMRB: 6749
• 分子名称: Paired amphipathic helix protein Sin3b, transcription factor REST (version 3) (2 entities in total)
• 機能のキーワード: nrsf, sin3, pah1, transcriptional repressor, gene regulation
• 由来する生物種: Mus musculus (house mouse); 詳細
• 細胞内の位置: Nucleus: Q62141; Nucleus (Probable): Q13127
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 10353.90

構造登録者

Nomura, M.,Uda-Tochio, H.,Murai, K.,Mori, N.,Nishimura, Y. (登録日: 2005-07-20, 公開日: 2005-12-20, 最終更新日: 2024-05-29)

主引用文献

Nomura, M.,Uda-Tochio, H.,Murai, K.,Mori, N.,Nishimura, Y.
The Neural Repressor NRSF/REST Binds the PAH1 Domain of the Sin3 Corepressor by Using its Distinct Short Hydrophobic Helix
J.Mol.Biol., 354:903-915, 2005

PubMed Abstract: 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.

PubMed: 16288918
DOI: 10.1016/j.jmb.2005.10.008

実験手法

SOLUTION NMR