Abstract
Background 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.
Highlights
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]
We recently solved a crystal structure of the two cGMP binding sites from PKG Ia in order to highlight the atomic details of the regulatory domain
This PKG78-355 structure is free of cGMP and presents the protein in an elongated conformation
Summary
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]. We recently solved a crystal structure of the two cGMP binding sites from PKG Ia in order to highlight the atomic details of the regulatory domain.
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