| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10871125 | FEBS Letters | 2013 | 5 Pages |
Abstract
⺠Structures of intact eNOS ± CaM have been derived from cryo-electron micrographs. ⺠The reductase domains appear to be mobile with respect to the oxygenase domain dimer. ⺠Densities consistent with oxygenase-docked FMN modules are observed in the presence of CaM. ⺠Additional densities are observed that are proposed to be bound and docked CaM. ⺠A novel model is suggested in which docking of CaM promotes docking of the FMN modules.
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Authors
Anthony Persechini, Quang-Kim Tran, D.J. Black, Edward P. Gogol,