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dc.contributor.advisorVan Doren, Stevenen
dc.contributor.authorDing, Zhaofeng, 1978-en_US
dc.date.issued2007eng
dc.date.submitted2007 Springen
dc.descriptionThe entire dissertation/thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file (which also appears in the research.pdf); a non-technical general description, or public abstract, appears in the public.pdf file.en_US
dc.descriptionTitle from title screen of research.pdf file (viewed on September 24, 2007)en_US
dc.descriptionVita.en_US
dc.descriptionIncludes bibliographical references.en_US
dc.descriptionThesis (Ph. D.) University of Missouri-Columbia 2007.en_US
dc.descriptionDissertations, Academic -- University of Missouri--Columbia -- Biochemistry (Agriculture)en_US
dc.description.abstractFHA domains are phosphoThr recognition modules found in diverse signaling proteins. Kinase-associated protein phosphatase (KAPP) from Arabidopsis employs its FHA domain in its negative regulation of some receptor-like kinase (RLK) signaling pathways. The interactions between the kinase-interacting FHA (KI-FHA) domain of KAPP and RLK kinase domains have been investigated. Three phosphoThr peptides of KAPP-binding RLKs were found by isothermal titration calorimetry (ITC) and NMR to bind KI-FHA, with Kd values of 8 to 30 [mu]M. Thermodynamics study revealed that their affinities were driven by favorable enthalpy and the hydrophobic effect. Mutagenesis of these three threonine sites suggests Thr546 in the C-lobe of BAK1 kinase domain to be a principal site of KI-FHA binding. BRI1 kinase domain interacts with the same 3/4, 4/5, 6/7, 8/9, and 10/11 recognition loops of KI-FHA as do phosphoThr peptides. The backbone mobility of KI-FHA, free and bound to pThr868CLV1 peptide has also been investigated using 15N NMR relaxation at 500 MHz and 600 MHz. Binding of the peptide seems to reduce nsec-scale fluctuations of KI-FHA globally. In the psec to nsec timescale, KI-FHA residues that are critical for phosphopeptide recognitions are rigid. Peptide binding rigidifies KI-FHA at the binding site and remote sites across the [beta-] sandwich. Peptide binding increases flexibility around the periphery of the binding site, perhaps relieving strain from the peptide association.en_US
dc.identifier.merlin.b59729776en_US
dc.identifier.oclc173259136en_US
dc.identifier.otherDingZ-020907-D7393en_US
dc.identifier.urihttp://hdl.handle.net/10355/4729
dc.publisherUniversity of Missouri--Columbiaen_US
dc.relation.ispartofcollection2007 Freely available dissertations (MU)
dc.relation.ispartofcommunityUniversity of Missouri-Columbia. Graduate School. Theses and Dissertations. Dissertations. 2007 Dissertations
dc.source.originalSubmitted by University of Missouri--Columbia Graduate School.eng
dc.subjectForkhead-associated domain.en_US
dc.subjectForkhead-associated domainen_US
dc.subject.lcshPlants -- Developmenten_US
dc.subject.lcshPhosphoprotein phosphatasesen_US
dc.subject.lcshProtein kinasesen_US
dc.subject.lcshNuclear magnetic resonanceen_US
dc.subject.lcshCellular signal transductionen_US
dc.subject.lcshMutagenesisen_US
dc.titleKinase-interacting FHA domain of kinase associated protein phosphatase: phosphopeptide interactions and NMR-detected dynamicsen_US
dc.typeThesisen_US
thesis.degree.disciplineBiochemistry (Agriculture) (MU)eng
thesis.degree.grantorUniversity of Missouri--Columbiaeng
thesis.degree.levelDoctoraleng
thesis.degree.namePh. D.eng


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