Search: onr:"swepub:oai:DiVA.org:uu-322707" >
Crystal structure o...
Crystal structure of human proteasome assembly chaperone PAC4 involved in proteasome formation
-
- Kurimoto, Eiji (author)
- Meijo Univ, Fac Pharm, Tempaku Ku, 150 Yagotoyama, Nagoya, Aichi 4688503, Japan.
-
- Satoh, Tadashi (author)
- Nagoya City Univ, Grad Sch Pharmaceut Sci, Mizuho Ku, Nagoya, Aichi 4678603, Japan.;JST, PRESTO, Mizuho Ku, Nagoya, Aichi 4678603, Japan.
-
- Ito, Yuri (author)
- Meijo Univ, Fac Pharm, Tempaku Ku, 150 Yagotoyama, Nagoya, Aichi 4688503, Japan.
-
show more...
-
- Ishihara, Eri (author)
- Meijo Univ, Fac Pharm, Tempaku Ku, 150 Yagotoyama, Nagoya, Aichi 4688503, Japan.
-
- Okamoto, Kenta (author)
- Uppsala universitet,Molekylär biofysik,Nagoya City Univ, Grad Sch Pharmaceut Sci, Mizuho Ku, Nagoya, Aichi 4678603, Japan
-
- Yagi-Utsumi, Maho (author)
- Nagoya City Univ, Grad Sch Pharmaceut Sci, Mizuho Ku, Nagoya, Aichi 4678603, Japan.;Natl Inst Nat Sci, Okazaki Inst Integrat Biosci, 5-1 Higashiyama, Okazaki, Aichi 4448787, Japan.;Natl Inst Nat Sci, Inst Mol Sci, 5-1 Higashiyama, Okazaki, Aichi 4448787, Japan.
-
- Tanaka, Keiji (author)
- Tokyo Metropolitan Inst Med Sci, Lab Prot Metab, Setagaya Ku, Tokyo 1568506, Japan.
-
- Kato, Koichi (author)
- Nagoya City Univ, Grad Sch Pharmaceut Sci, Mizuho Ku, Nagoya, Aichi 4678603, Japan.;Natl Inst Nat Sci, Okazaki Inst Integrat Biosci, 5-1 Higashiyama, Okazaki, Aichi 4448787, Japan.;Natl Inst Nat Sci, Inst Mol Sci, 5-1 Higashiyama, Okazaki, Aichi 4448787, Japan.
-
show less...
-
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. (creator_code:org_t)
- 2017-03-16
- 2017
- English.
-
In: Protein Science. - : WILEY. - 0961-8368 .- 1469-896X. ; 26:5, s. 1080-1085
- Related links:
-
https://onlinelibrar...
-
show more...
-
https://urn.kb.se/re...
-
https://doi.org/10.1...
-
show less...
Abstract
Subject headings
Close
- 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.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Cell- och molekylärbiologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Cell and Molecular Biology (hsv//eng)
Keyword
- assembly chaperone
- crystal structure
- PAC4
- proteasome
Publication and Content Type
- ref (subject category)
- art (subject category)
Find in a library
To the university's database