1AVO

PROTEASOME ACTIVATOR REG(ALPHA)

1AVO の概要

• エントリーDOI: 10.2210/pdb1avo/pdb
• 分子名称: 11S REGULATOR (2 entities in total)
• 機能のキーワード: proteasome activator, cell adhesion, interferon induction
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 161508.30

構造登録者

Hill, C.P.,Knowlton, J.R. (登録日: 1997-09-18, 公開日: 1997-12-31, 最終更新日: 2024-02-07)

主引用文献

Knowlton, J.R.,Johnston, S.C.,Whitby, F.G.,Realini, C.,Zhang, Z.,Rechsteiner, M.,Hill, C.P.
Structure of the proteasome activator REGalpha (PA28alpha).
Nature, 390:639-643, 1997

PubMed Abstract: The specificity of the 20S proteasome, which degrades many intracellular proteins, is regulated by protein complexes that bind to one or both ends of the cylindrical proteasome structure. One of these regulatory complexes, the 11S regulator (known as REG or PA28), stimulates proteasome peptidase activity and enhances the production of antigenic peptides for presentation by class I molecules of the major histocompatibility complex (MHC). The three REG subunits that have been identified, REGalpha, REGbeta and REGgamma (also known as the Ki antigen), share extensive sequence similarity, apart from a highly variable internal segment of 17-34 residues which may confer subunit-specific properties. REGalpha and REGbeta preferentially form a heteromeric complex, although purified REGalpha forms a heptamer in solution and has biochemical properties similar to the heteromeric REGalpha/REGbeta complex. We have now determined the crystal structure of human recombinant REGalpha at 2.8 A resolution. The heptameric barrel-shaped assembly contains a central channel that has an opening of 20 A diameter at one end and another of 30 A diameter at the presumed proteasome-binding surface. The binding of REG probably causes conformational changes that open a pore in the proteasome alpha-subunits through which substrates and products can pass.

PubMed: 9403698
DOI: 10.1038/37670

実験手法

X-RAY DIFFRACTION (2.8 Å)