Abstract
Cyclic GMP (cGMP) is a second messenger for cellular regulation and activates cGMP-dependent protein kinase (cG-PK). cG-PK, a homo-dimer of 150 kDa, has four partially cooperative binding sites for cGMP with KD-values in the order of 10 to 200 nM as has been shown by binding studies with 3H-cGMP1,2. Two types of sites have been described, site 1 with high affinity and slow dissociation and site 2 with lower affinity and faster dissociation. The primary structure of the enzyme has been reported and assigned to functional domains3.
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© 1987 Plenum Press, New York
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Ruf, H.H., Rack, M., Landgraf, W., Hofmann, F. (1987). Binding of Fluorescent Analogs of Cyclic GMP to cGMP-Dependent Protein Kinase. In: Heilmeyer, L.M.G. (eds) Signal Transduction and Protein Phosphorylation. NATO ASI Series, vol 135. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-0166-1_13
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DOI: https://doi.org/10.1007/978-1-4757-0166-1_13
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