Kinase interaction domain of kinase-associated protein phosphatase, a phosphoprotein-binding domain.

ABSTRACT: Kinase-associated protein phosphatase interacts specifically with plant receptor-like protein kinases. This interaction is thought to be a key step in signal perception and transduction. The minimal kinase interaction (KI) domain of kinase-associated protein phosphatase was mapped to a 119-aa segment spanning residues 180 to 298. A forkhead-associated (FHA) homology region resides in this minimal KI domain. Site-directed mutagenesis of four highly conserved sites in this FHA homology region abolishes the KI domain's interaction with receptor-like protein kinases, indicating that the FHA region is essential for binding. Serial deletion analysis indicates that 30 aa on each side of the FHA region are also needed for binding; this minimal functional unit is designated as the KI domain. Kineti

SUBMITTER: Li J 

PROVIDER: S-EPMC22145 | biostudies-literature | 1999 Jul

REPOSITORIES: biostudies-literature