ArticleProceedings of the National Academy of Sciences of the United States of America2003
NMR structure of the forkhead-associated domain from the Arabidopsis receptor kinase-associated protein phosphatase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 38 citations in OpenAlex.
- The role of forkhead-associated (FHA)-domain proteins in plant biology.Plant molecular biology · 2023Review
- Molecular convergence by differential domain acquisition is a hallmark of chromosomal passenger complex evolution.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Crystal Structure of FOXC2 in Complex with DNA Target.ACS omega · 2019Article
- The molecular basis of ATM-dependent dimerization of the Mdc1 DNA damage checkpoint mediator.Nucleic acids research · 2012Article
- Mechanism of PhosphoThreonine/Serine Recognition and Specificity for Modular Domains from All-atom Molecular Dynamics.BMC biophysics · 2011Article
- Phosphorylation-independent dual-site binding of the FHA domain of KIF13 mediates phosphoinositide transport via centaurin alpha1.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- NMR and bioinformatics discovery of exosites that tune metalloelastase specificity for solubilized elastin and collagen triple helices.The Journal of biological chemistry · 2010Article
- Protein phosphatase complement in rice: genome-wide identification and transcriptional analysis under abiotic stress conditions and reproductive development.BMC genomics · 2010Article
- Mechanistic insights into phosphoprotein-binding FHA domains.Accounts of chemical research · 2008Review
- Partially unfolded forms and non-two-state folding of a beta-sandwich: FHA domain from Arabidopsis receptor kinase-associated protein phosphatase.Journal of molecular biology · 2006Article
- DAWDLE, a forkhead-associated domain gene, regulates multiple aspects of plant development.Plant physiology · 2006Article
- PhosphoThr peptide binding globally rigidifies much of the FHA domain from Arabidopsis receptor kinase-associated protein phosphatase.Biochemistry · 2005Article
- Evolutionary trace analysis of the alpha-D-phosphohexomutase superfamily.Protein science : a publication of the Protein Society · 2004Article
- Isolation and developmental expression of Xenopus FoxJ1 and FoxK1.Development genes and evolution · 2004Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.