ACTIVITY MODULATION OF PROTEIN KINASE AND PHOSPHATASE

蛋白激酶和磷酸酶的活性调节

• 批准号: 8362286
• 负责人: Jialin Charles Zheng
• 金额: $ 0.03万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-03-01 至 2012-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8362286
• 关键词: Biological; Calcineurin; Calmodulin; Complex; Eukaryota; Event; Funding; Grant; Length; Life; Membrane; Molecular Conformation; National Center for Research Resources; Organism; Phosphoric Monoester Hydrolases; Phosphorylation; Phosphotransferases; Principal Investigator; Protein Dephosphorylation; Protein Kinase; Protein phosphatase; Radiation; Research; Research Infrastructure; Resources; Signal Transduction; Source; Structure; United States National Institutes of Health; base; chemical reaction; cost; extracellular; mutant; structural biology

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Phosphorylation/dephosphorylation is the most crucial chemical reaction taking place in living organisms, which is the basis for the regulatory control of many diverse biological events triggered by extracellular effectors. Our project involves the determination of the crystal structures of two protein kinases, AceK (also a protein phosphatase) and Etk, and a protein phosphatase, calcineurin. For AceK, which possesses both kinase and phosphatase activities, the kinase and phosphatase conformations of AceK, as well as AceK-ICDH complex structures will be solved for investigating the AceK activity switch and regulatory mechanism. The structures of full length membrane Etk, its mutants, and its complex with substrate Ugd will be determined. For calcineurin, which is a calmodulin-activated central controller of signaling in eukaryotes, we have created a fusion construct (known as CBA) to facilitate the structure determination of calmodulin-calcineurin complex, which would represent a structure of calmodulin in complex with an intact substrate.

这个子项目是利用这些资源的众多研究子项目之一