Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 285, Issue 43, Pages 32684-32688Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.C110.161430
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Funding
- National Institutes of Health [R01-AR051300, K22-CA124517]
- American Heart Grant [09SDG2150143]
- National Institutes of Health (NIGMS)
- Howard Hughes Medical Institute
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Cyclic GMP-dependent protein kinase (PKG) is a key mediator of the nitric oxide/cGMP signaling pathway and plays a central role in regulating cardiovascular and neuronal functions. The N-terminal similar to 50 amino acids of the kinase are required for homodimerization and association with isoform-specific PKG-anchoring proteins (GKAPs), which target the kinase to specific substrates. To understand the molecular details of PKG dimerization and gain insight into its association with GKAPs, we solved a crystal structure of the PKG I beta dimerization/docking domain. Our structure provides molecular details of this unique leucine/isoleucine zipper, revealing specific hydrophobic and ionic interactions that mediate dimerization and demonstrating the topology of the GKAP interaction surface.
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