Site I Inactivation Impacts Calmodulin Calcium Binding and Activation of Bordetella pertussis Adenylate Cyclase Toxin

Site I inactivation of calmodulin (CaM) was used to examine the importance of aspartic acid 22 at position 3 in CaM calcium binding, protein folding, and activation of the Bordetella pertussis adenylate cyclase toxin domain (CyaA-ACD). NMR calcium titration experiments showed that site I in the CaM...

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Detalles Bibliográficos
Autores principales: Johns, Christian W., Finley, Natosha L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2017
Materias:
Communication
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5744109/
https://www.ncbi.nlm.nih.gov/pubmed/29189743
http://dx.doi.org/10.3390/toxins9120389

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5744109/
https://www.ncbi.nlm.nih.gov/pubmed/29189743
http://dx.doi.org/10.3390/toxins9120389

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