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Crystal structure o...
Crystal structure of human proteasome assembly chaperone PAC4 involved in proteasome formation
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- Kurimoto, Eiji (författare)
- Meijo Univ, Fac Pharm, Tempaku Ku, 150 Yagotoyama, Nagoya, Aichi 4688503, Japan.
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- Satoh, Tadashi (författare)
- Nagoya City Univ, Grad Sch Pharmaceut Sci, Mizuho Ku, Nagoya, Aichi 4678603, Japan.;JST, PRESTO, Mizuho Ku, Nagoya, Aichi 4678603, Japan.
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- Ito, Yuri (författare)
- Meijo Univ, Fac Pharm, Tempaku Ku, 150 Yagotoyama, Nagoya, Aichi 4688503, Japan.
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- Ishihara, Eri (författare)
- Meijo Univ, Fac Pharm, Tempaku Ku, 150 Yagotoyama, Nagoya, Aichi 4688503, Japan.
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- Okamoto, Kenta (författare)
- Uppsala universitet,Molekylär biofysik,Nagoya City Univ, Grad Sch Pharmaceut Sci, Mizuho Ku, Nagoya, Aichi 4678603, Japan
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- Yagi-Utsumi, Maho (författare)
- 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.
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- Tanaka, Keiji (författare)
- Tokyo Metropolitan Inst Med Sci, Lab Prot Metab, Setagaya Ku, Tokyo 1568506, Japan.
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- Kato, Koichi (författare)
- 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.
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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
- Engelska.
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Ingår i: Protein Science. - : WILEY. - 0961-8368 .- 1469-896X. ; 26:5, s. 1080-1085
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Cell- och molekylärbiologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Cell and Molecular Biology (hsv//eng)
Nyckelord
- assembly chaperone
- crystal structure
- PAC4
- proteasome
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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