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The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1.

Molecular cell | Nov 14, 1999

The small G protein Rho has emerged as a key regulator of cellular events involving cytoskeletal reorganization. Here we report the 2.2 A crystal structure of RhoA bound to an effector domain of protein kinase PKN/PRK1. The structure reveals the antiparallel coiled-coil finger (ACC finger) fold of the effector domain that binds to the Rho specificity-determining regions containing switch I, beta strands B2 and B3, and the C-terminal alpha helix A5, predominantly by specific hydrogen bonds. The ACC finger fold is distinct from those for other small G proteins and provides evidence for the diverse ways of effector recognition. Sequence analysis based on the structure suggests that the ACC finger fold is widespread in Rho effector proteins.

Pubmed ID: 10619026 RIS Download

Mesh terms: Amino Acid Motifs | Amino Acid Sequence | Amino Acid Substitution | Binding Sites | Catalytic Domain | Crystallography, X-Ray | Guanosine 5'-O-(3-Thiotriphosphate) | Humans | Hydrogen Bonding | Leucine Zippers | Magnesium | Models, Molecular | Molecular Sequence Data | Protein Binding | Protein Kinase C | Protein Structure, Secondary | Sequence Alignment | Sequence Homology, Amino Acid | Structure-Activity Relationship | rhoA GTP-Binding Protein