X-RAY CRYSTALLOGRAPHIC STUDIES OF RIBOSOMAL S6 KINASE 2 (RSK2)

核糖体 S6 激酶 2 (RSK2) 的 X 射线晶体学研究

• 批准号: 8169266
• 负责人: ZIGANG DONG
• 金额: $ 0.7万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-04-01 至 2011-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8169266
• 关键词: Cell Proliferation; Coffin-Lowry syndrome; Computer Retrieval of Information on Scientific Projects Database; Data; Family; Funding; Gene Mutation; Grant; Growth Factor; Homologous Gene; Human; Institution; Length; Mitogens; Molecular Structure; Pathway interactions; Phosphotransferases; Protein-Serine-Threonine Kinases; Proteins; Research; Research Personnel; Resources; Roentgen Rays; Source; Stress; Structure; United States National Institutes of Health; cancer cell; meetings; research study; response; ribosomal protein S6 kinase 2

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The 90-kDa ribosomal S6 kinase 2 (RSK2) is important serine-threonine kinase broadly expressed in response to various growth factors. RSK pathway is a key regulator of cancer cell proliferation. In humans, RSK2 gene mutations are manifested in Coffin-Lowry syndrome characterized by severe psychomotor retardation. Elucidating the molecular structure of full length RSK2 is essential for understanding its activation mechanism. RSK2 belongs to the family of unusual serine-threonine kinases that contain two distinct kinase domains connected by a linker region. The mitogen- and stress-reguated kinase 1 (MSK1) is close homologue to RSK2 with the same domain organization. The crystal structure of both proteins, RSK2 and MSK1 are not available. We plan to determine crystals structure of full length RSK2 and MSK1. We will need to perform anomalous diffraction experiments at Se-edge energy for Se/Met protein in order to get the data for Se/Met full length MSK1, which is already purified.

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