Biochemical and crystallographic characterization of a Rho effector domain of the protein serine/threonine kinase N in a complex with RhoA.

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Citation

Maesaki R, Shimizu T, Ihara K, Kuroda S, Kaibuchi K, Hakoshima T

Biochemical and crystallographic characterization of a Rho effector domain of the protein serine/threonine kinase N in a complex with RhoA.

J Struct Biol. 1999 Jun 15;126(2):166-70.

PubMed ID
10388627 [ View in PubMed
]
Abstract

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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Transforming protein RhoAP61586Details
Serine/threonine-protein kinase N1Q16512Details