3nmd | pdb_00003nmd

Crystal structure of the leucine zipper domain of cGMP dependent protein kinase I beta

spinqualitylabelsall models 3nmd, resolution 2.27Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3nmd is a 5 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, HEZ NonStd Res: MSE Gene: PRKG1 (Homo sapiens) Resources: FirstGlance, OCA, RCSB, PDBsum 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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