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- Kurimoto, Eiji, et al.
(författare)
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Crystal structure of human proteasome assembly chaperone PAC4 involved in proteasome formation
- 2017
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Ingår i: Protein Science. - : WILEY. - 0961-8368 .- 1469-896X. ; 26:5, s. 1080-1085
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Tidskriftsartikel (refereegranskat)abstract
- The 26S proteasome is a large protein complex, responsible for degradation of ubiquinated proteins in eukaryotic cells. Eukaryotic proteasome formation is a highly ordered process that is assisted by several assembly chaperones. The assembly of its catalytic 20S core particle depends on at least five proteasome-specific chaperones, i.e., proteasome-assembling chaperons 1-4 (PAC1-4) and proteasome maturation protein (POMP). The orthologues of yeast assembly chaperones have been structurally characterized, whereas most mammalian assembly chaperones are not. In the present study, we determined a crystal structure of human PAC4 at 1.90-angstrom resolution. Our crystallographic data identify a hydrophobic surface that is surrounded by charged residues. The hydrophobic surface is complementary to that of its binding partner, PAC3. The surface also exhibits charge complementarity with the proteasomal 4-5 subunits. This will provide insights into human proteasome-assembling chaperones as potential anticancer drug targets.
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