Structural and Functional Characterization of an Anesthetic Binding Site in the Second Cysteine-Rich Domain of Protein Kinase Cδ(∗)

Elucidating the principles governing anesthetic-protein interactions requires structural determinations at high resolutions not yet achieved with ion channels. Protein kinase C (PKC) activity is modulated by general anesthetics. We solved the structure of the phorbol-binding domain (C1B) of PKCδ com...

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Autori principali: Shanmugasundararaj, Sivananthaperumal, Das, Joydip, Sandberg, Warren S., Zhou, Xiaojuan, Wang, Dan, Messing, Robert O., Bruzik, Karol S., Stehle, Thilo, Miller, Keith W.
Natura: Artigo
Lingua:Inglês
Pubblicazione: The Biophysical Society 2012
Soggetti:
Proteins and Nucleic Acids
Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC3514512/
https://ncbi.nlm.nih.gov/pubmed/23283232
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bpj.2012.10.034
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