期刊
MOLECULAR & CELLULAR PROTEOMICS
卷 9, 期 8, 页码 1666-1677出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/mcp.R000002-MCP201
关键词
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资金
- European Commission
- Deutsche Forschungsgemeinschaft Cluster of Excellence Munich-Centre for Advanced Photonics
- National Institutes of Health [R01 GM54762, U54 RR022220, PN2 EY016525, R01 GM083960]
- Human Frontier Science Project Organization
- Clore Foundation
- Sandler Family Supporting Foundation
- National Science Foundation [IIS-0705196]
- Ron Conway
- Mike Homer
- Hewlett-Packard
- NetApp
- IBM
- Intel
The 26S proteasome is the end point of the ubiquitin-proteasome pathway and degrades ubiquitylated substrates. It is composed of the 20S core particle (CP), where degradation occurs, and the 19S regulatory particle (RP), which ensures substrate specificity of degradation. Whereas the CP is resolved to atomic resolution, the architecture of the RP is largely unknown. We provide a comprehensive analysis of the current structural knowledge on the RP, including structures of the RP subunits, physical protein-protein interactions, and cryoelectron microscopy data. These data allowed us to compute an atomic model for the CP-AAA-ATPase subcomplex. In addition to this atomic model, further subunits can be mapped approximately, which lets us hypothesize on the substrate path during its degradation. Molecular & Cellular Proteomics 9: 1666-1677, 2010.
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