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NMR structure of kinase-interacting FHA domain of kinase associated protein phosphatase, KAPP in Arabidopsis
Structural highlights
FunctionP2C70_ARATH Dephosphorylates the Ser/Thr receptor-like kinase RLK5. May function as a signaling component in a pathway involving RLK5 (PubMed:15592873). Binds and dephosphorylates CLAVATA1 (CLV1). Functions as a negative regulator of the CLV1 signaling in plant development (PubMed:9294234, PubMed:9701578). Dephosphorylates SERK1 receptor kinase on threonine residues in the A-loop. Dephosphorylation of SERK1 controls SERK1 internalization (PubMed:12101128). Component of a signaling pathway which mediates adaptation to NaCl stress. Is not a component of the SALT OVERLY SENSITIVE (SOS) pathway (PubMed:18162596).[1] [2] [3] [4] [5] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedForkhead-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. 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[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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