1mzk
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NMR structure of kinase-interacting FHA domain of kinase associated protein phosphatase, KAPP in Arabidopsis
OverviewOverview
Forkhead-associated (FHA) domains are phosphoprotein-binding modules found, in diverse signaling proteins that bind partners phosphorylated on, threonine or serine. Kinase-associated protein phosphatase from, Arabidopsis employs its FHA domain for negative regulation of, receptor-like kinase signaling pathways, which are important in plant, development. The solution structure of the free state of, kinase-interacting FHA domain (KI-FHA) of kinase-associated protein, phosphatase has been determined with high precision and accuracy using, residual dipolar couplings. KI-FHA is a sandwich of a five-stranded mixed, beta-sheet with a six-stranded antiparallel beta-sheet. Despite homology, only in the recognition loops, this fold is shared with FHA domains from, checkpoint proteins from yeast and humans, as well as with nonhomologous, MH2 domains of Smad tumor suppressors. A shared pattern of hydrophobicity, throughout FHA domains and Smad MH2 domains may stabilize the core of the, beta-sandwich. Evolutionary trace analysis of FHA domains suggests, class-specific residues in the recognition loops that could tune their, phosphoprotein-binding specificity. This surface agrees with that of, KI-FHA in contact with a phosphothreonine peptide ligand. Evolutionary, trace analysis also predicts an unexpected swath of class-specific, residues on another face of FHA domains. Protein interactions with these, faces may affect assembly of transmembrane signaling complexes in plants, and in other FHA domain-containing assemblies.
About this StructureAbout this Structure
1MZK is a Single protein structure of sequence from Arabidopsis thaliana. Active as Phosphoprotein phosphatase, with EC number 3.1.3.16 Full crystallographic information is available from OCA.
ReferenceReference
NMR structure of the forkhead-associated domain from the Arabidopsis receptor kinase-associated protein phosphatase., Lee GI, Ding Z, Walker JC, Van Doren SR, Proc Natl Acad Sci U S A. 2003 Sep 30;100(20):11261-6. Epub 2003 Sep 18. PMID:14500786
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