3NMD

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

3NMD の概要

• エントリーDOI: 10.2210/pdb3nmd/pdb
• 分子名称: cGMP Dependent PRotein Kinase, HEXANE-1,6-DIOL, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: leucine zipper, coiled-coil, structural genomics, berkeley structural genomics center, bsgc, dimerization, inositol triphosphate receptor-associated pkg substrate, transcriptional regulator tfii-i, transferase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 44556.10

構造登録者

Kim, C.,Casteel, D.E.,Smith-Nguyen, E.V.,Sankaran, B.,Berkeley Structural Genomics Center (BSGC) (登録日: 2010-06-22, 公開日: 2010-09-08, 最終更新日: 2024-10-30)

主引用文献

Casteel, D.E.,Smith-Nguyen, E.V.,Sankaran, B.,Roh, S.H.,Pilz, R.B.,Kim, C.
A crystal structure of the cyclic GMP-dependent protein kinase I{beta} dimerization/docking domain reveals molecular details of isoform-specific anchoring.
J.Biol.Chem., 285:32684-32688, 2010

PubMed Abstract: 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 ∼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 Iβ 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.

PubMed: 20826808
DOI: 10.1074/jbc.C110.161430

実験手法

X-RAY DIFFRACTION (2.272 Å)