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dc.contributor.advisorVan Doren, Steveneng
dc.contributor.authorDing, Zhaofeng, 1978-eng
dc.date.issued2007eng
dc.date.submitted2007 Springeng
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.eng
dc.descriptionTitle from title screen of research.pdf file (viewed on September 24, 2007)eng
dc.descriptionVita.eng
dc.descriptionIncludes bibliographical references.eng
dc.descriptionThesis (Ph. D.) University of Missouri-Columbia 2007.eng
dc.descriptionDissertations, Academic -- University of Missouri--Columbia -- Biochemistry (Agriculture)eng
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.eng
dc.identifier.merlin.b59729776eng
dc.identifier.oclc173259136eng
dc.identifier.otherDingZ-020907-D7393eng
dc.identifier.urihttp://hdl.handle.net/10355/4729eng
dc.languageEnglisheng
dc.publisherUniversity of Missouri--Columbiaeng
dc.relation.ispartofcollection2007 Freely available dissertations (MU)eng
dc.relation.ispartofcommunityUniversity of Missouri-Columbia. Graduate School. Theses and Dissertations. Dissertations. 2007 Dissertationseng
dc.source.originalSubmitted by University of Missouri--Columbia Graduate School.eng
dc.subjectForkhead-associated domain.eng
dc.subjectForkhead-associated domaineng
dc.subject.lcshPlants -- Developmenteng
dc.subject.lcshPhosphoprotein phosphataseseng
dc.subject.lcshProtein kinaseseng
dc.subject.lcshNuclear magnetic resonanceeng
dc.subject.lcshCellular signal transductioneng
dc.subject.lcshMutagenesiseng
dc.titleKinase-interacting FHA domain of kinase associated protein phosphatase: phosphopeptide interactions and NMR-detected dynamicseng
dc.typeThesiseng
thesis.degree.disciplineBiochemistry (Agriculture) (MU)eng
thesis.degree.grantorUniversity of Missouri--Columbiaeng
thesis.degree.levelDoctoraleng
thesis.degree.namePh. D.eng


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