Biochemical and crystallographic characterization of a Rho effector domain of the protein serine/threonine kinase N in a complex with RhoA.
The effector domain of human protein serine/threonine kinase N (PKN), an effector protein for the small GTP-binding protein Rho, was expressed and purified for protein characterization and crystallization in a complex form with human RhoA. In solution, RhoA binds to the PKN effector domain with 1:2 stoichiometry in a GTP-dependent manner. The obtained complex crystals diffract to 2.2 A resolution.
Maesaki
R
R
Division of Structural Biology, Division of Signal Transduction, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara, 630-0101, Japan.
Shimizu
T
T
Ihara
K
K
Kuroda
S
S
Kaibuchi
K
K
Hakoshima
T
T
D002850:Chromatography, Gel; D003460:Crystallization; D019204:GTP-Binding Proteins / Q000737:chemistry*; D016244:Guanosine 5'-O-(3-Thiotriphosphate) / Q000737:chemistry; D006801:Humans; D010446:Peptide Fragments / Q000737:chemistry; D011485:Protein Binding; D011493:Protein Kinase C; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry*; D011505:Protein-Tyrosine Kinases / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry; D014961:X-Ray Diffraction
D010446:Peptide Fragments; D011994:Recombinant Proteins; D016244:Guanosine 5'-O-(3-Thiotriphosphate); C061570:protein kinase N; D011505:Protein-Tyrosine Kinases; D017346:Protein Serine-Threonine Kinases; D011493:Protein Kinase C; D019204:GTP-Binding Proteins