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Crystal structure of human proteasome assembly chaperone PAC4 involved in proteasome formation
Meijo Univ, Fac Pharm, Tempaku Ku, 150 Yagotoyama, Nagoya, Aichi 4688503, Japan..
Nagoya City Univ, Grad Sch Pharmaceut Sci, Mizuho Ku, Nagoya, Aichi 4678603, Japan.;JST, PRESTO, Mizuho Ku, Nagoya, Aichi 4678603, Japan..
Meijo Univ, Fac Pharm, Tempaku Ku, 150 Yagotoyama, Nagoya, Aichi 4688503, Japan..
Meijo Univ, Fac Pharm, Tempaku Ku, 150 Yagotoyama, Nagoya, Aichi 4688503, Japan..
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2017 (English)In: Protein Science, ISSN 0961-8368, E-ISSN 1469-896X, Vol. 26, no 5, 1080-1085 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
WILEY , 2017. Vol. 26, no 5, 1080-1085 p.
Keyword [en]
assembly chaperone, crystal structure, PAC4, proteasome
National Category
Cell and Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-322707DOI: 10.1002/pro.3153ISI: 000400166800015PubMedID: 28263418OAI: oai:DiVA.org:uu-322707DiVA: diva2:1104669
Available from: 2017-06-01 Created: 2017-06-01 Last updated: 2017-06-01Bibliographically approved

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