PMID: 7537829Apr 28, 1995Paper

The human proteasome subunit HsN3 is located in the inner rings of the complex dimer

Journal of Molecular Biology
F KoppB Dahlmann

Abstract

Subunit HsN3 of the human proteasome is a beta-type subunit homologous to PRE4 from yeast, X1 beta from Xenopus and RN3 from the rat. Using electron microscopy, the binding sites of a monoclonal antibody with specificity for subunit HsN3 have been located in the two juxtaposed inner rings of the human proteasome. Subunit HsN3 was present in two copies, one in each ring, in accordance with our concept of two identical halves making up the complete human proteasome. The subunit is involved in the trypsin-like as well as the peptidylglutamyl-peptide cleavage activities.

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Citations

May 22, 2001·Archives of Biochemistry and Biophysics·R Hartmann-PetersenK B Hendil
May 14, 2003·Journal of Molecular Biology·Friedrich Kopp, Lothar Kuehn
Jul 15, 1998·Mechanisms of Ageing and Development·T Hayashi, S Goto
Aug 1, 1996·Current Opinion in Biotechnology·D StockJ Löwe
Apr 1, 1997·Current Opinion in Structural Biology·W Baumeister, A Lupas
Apr 1, 1997·Proceedings of the National Academy of Sciences of the United States of America·F KoppW Uerkvitz
Jan 1, 1996·Journal of Acquired Immune Deficiency Syndromes and Human Retrovirology : Official Publication of the International Retrovirology Association·C Béraud, W C Greene
Oct 26, 2010·Molecular and Biochemical Parasitology·William MathiesonR Alan Wilson
Apr 18, 2009·Molecular Aspects of Medicine·Tobias JungTilman Grune
Feb 6, 1998·Journal of Molecular Biology·W L GerardsW Boelens

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