4R4L

Crystal structure of wt cGMP dependent protein kinase I alpha (PKGI alpha) leucine zipper

Summary for 4R4L

• Entry DOI: 10.2210/pdb4r4l/pdb
• Related: 1ZXA 3NMD 4OJK 4R4M
• Descriptor: cGMP-dependent protein kinase 1, HEXANE-1,6-DIOL, SULFATE ION, ... (4 entities in total)
• Functional Keywords: leucine zipper, kinase, binding domain, mypt1, rhoa, dna binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm : Q13976
• Total number of polymer chains: 3
• Total formula weight: 17974.89

Authors

Reger, A.S.,Guo, E.,Yang, M.P.,Qin, L.,Kim, C. (deposition date: 2014-08-19, release date: 2015-09-23, Last modification date: 2024-11-06)

Primary citation

Qin, L.,Reger, A.S.,Guo, E.,Yang, M.P.,Zwart, P.,Casteel, D.E.,Kim, C.
Structures of cGMP-Dependent Protein Kinase (PKG) I alpha Leucine Zippers Reveal an Interchain Disulfide Bond Important for Dimer Stability.
Biochemistry, 54:4419-4422, 2015

PubMed Abstract: cGMP-dependent protein kinase (PKG) Iα is a central regulator of smooth muscle tone and vasorelaxation. The N-terminal leucine zipper (LZ) domain dimerizes and targets PKG Iα by interacting with G-kinase-anchoring proteins. The PKG Iα LZ contains C42 that is known to form a disulfide bond upon oxidation and to activate PKG Iα. To understand the molecular details of the PKG Iα LZ and C42-C42' disulfide bond, we determined crystal structures of the PKG Iα wild-type (WT) LZ and C42L LZ. Our data demonstrate that the C42-C42' disulfide bond dramatically stabilizes PKG Iα and that the C42L mutant mimics the oxidized WT LZ structurally.

PubMed: 26132214
DOI: 10.1021/acs.biochem.5b00572

Experimental method

X-RAY DIFFRACTION (2.245 Å)