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Calmodulin-induced structural changes in endothelial nitric oxide synthase
We have derived structures of intact calmodulin(CaM)-free and CaM-bound endothelial nitric oxide synthase (eNOS) by reconstruction from cryo-electron micrographs. The CaM-free reconstruction is well fitted by the oxygenase domain dimer, but the reductase domains are not visible, suggesting they are...
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| Main Authors: | , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
2012
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3569036/ https://ncbi.nlm.nih.gov/pubmed/23266515 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.febslet.2012.12.012 |
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