Structural Basis for the Activation of Proteasomes by 11S Regulators

By F. Whitby, E. Masters, L. Kramer, J. Knowlton, Y. Yao, Ching C. Wang, Christopher P. Hill. 2000

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Relating whole-genome expression data with protein-protein interactions. (2002, background): “An investigation of the crystal structure of 20S particle (Whitby et al. 2000) did not reveal any relationship with the gene expression differences (e.g., proteins with slightly more random correlations tending to be more on the surface of the particle).”
Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome (2009, background): “However, the ability of the proteasome to act as an endoprotease on large substrates (97), and related studies (98, 99), have shown that the CP channel can accommodate two peptide segments, and this conclusion is consistent with the size of the channel as determined by crystallography (6, 8).”
Proteasome inhibitors: from research tools to drug candidates. (2001, background): “Location of the N-termini of K subunits, which are responsible for closing the channel, are shown according to the structure of yeast proteasome with PA26 activator from Trypanosoma brucei, which is the structural homologue of the mammalian PA28 activator [152].”
The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. (2002, background): “PA28 probably activates the CP by binding to the -ring surface and rearranging the blocking NH2 termini (469).”