3nmd

Publication Abstract from PubMed

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 approximately 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 Ibeta 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.

A crystal structure of the cyclic GMP-dependent protein kinase I{beta} dimerization/docking domain reveals molecular details of isoform-specific anchoring.,Casteel DE, Smith-Nguyen EV, Sankaran B, Roh SH, Pilz RB, Kim C J Biol Chem. 2010 Oct 22;285(43):32684-8. Epub 2010 Sep 8. PMID:20826808^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.