期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 109, 期 34, 页码 13555-13560出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1207493109
关键词
copper transport; protein maturation; protein-protein interactions
资金
- Programmi di Ricerca di Rilevante Interesse Nazionale (PRIN) [2009FAKHZT_001]
- Bio-NMR (European Commission Framework Programme 7 e-Infrastructure grant) [261863]
- Estonian Science Foundation [8811]
- Ente Cassa di Risparmio di Firenze
Copper chaperone for superoxide dismutase 1 (SOD1), CCS, is the physiological partner for the complex mechanism of SOD1 maturation. We report an in vitro model for human CCS-dependent SOD1 maturation based on the study of the interactions of human SOD1 (hSOD1) with full-length WT human CCS (hCCS), as well as with hCCS mutants and various truncated constructs comprising one or two of the protein's three domains. The synergy between electrospray ionization mass spectrometry (ESI-MS) and NMR is fully exploited. This is an in vitro study of this process at the molecular level. Domain 1 of hCCS is necessary to load hSOD1 with Cu(I), requiring the heterodimeric complex formation with hSOD1 fostered by the interaction with domain 2. Domain 3 is responsible for the catalytic formation of the hSOD1 Cys-57-Cys-146 disulfide bond, which involves both hCCS Cys-244 and Cys-246 via disulfide transfer.
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