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A structural analysis of the regulatory domain from the cGMP-dependent protein kinase Iα
© Osborne et al; licensee BioMed Central Ltd. 2011
Published: 1 August 2011
The cGMP-dependent protein kinase (PKG) has two tandem cyclic nucleotide binding (CNB) domains which act as the primary intracellular receptor for cGMP [1, 2]. PKG exhibits a homodimeric rod-like structure which undergoes significant molecular rearrangements upon the binding of cGMP [3–5]. However, a detailed structural analysis of the core regulatory elements inherent to PKG is still required.
Overall, these studies provide the first atomic resolution model of tandem cGMP binding domains and expand our understanding of the allosteric mechanisms surrounding PKG activation.
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