MECHANISTIC INSIGHTS INTO THE REGULATION OF AN MTB PROTEIN TYROSINE PHOSPHATASE
MTB 蛋白酪氨酸磷酸酶调节机制的见解
基本信息
- 批准号:7598224
- 负责人:
- 金额:$ 0.02万
- 依托单位:
- 依托单位国家:美国
- 项目类别:
- 财政年份:2007
- 资助国家:美国
- 起止时间:2007-03-01 至 2008-02-29
- 项目状态:已结题
- 来源:
- 关键词:Active SitesAffectCell physiologyComputer Retrieval of Information on Scientific Projects DatabaseFundingGrantImmuneImmune responseImmune systemInstitutionMediatingMycobacterium InfectionsMycobacterium tuberculosisProtein BindingProtein DephosphorylationProtein Tyrosine PhosphataseProteinsReactive Oxygen SpeciesRegulationResearchResearch PersonnelResourcesRoleSignal TransductionSignal Transduction PathwaySourceTyrosine PhosphorylationUnited States National Institutes of Healthinhibitor/antagonistinsightmutantoxidationpathogenresponse
项目摘要
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.
Tyrosine phosphorylation is an important signal that tightly regulates many cellular responses mediated by the immune system. Protein tyrosine phosphatases (PTP) antagonize these key signal transduction pathways though their intrinsic dephosphorylation activity. Intracellular pathogens, such as Mycobacterium tuberculosis (Mtb), may secrete PTPs to evade host responses or achieve immune escape. The catalytic mechanisms, cellular functions and host substrates of the two Mtb PTPs (PtpA and PtpB) are largely unknown. I will investigate PtpB¿s autoinhibitory lid, a structural feature that blocks potential substrates as well as reactive oxygen species (ROS) access to the protein¿s active site. I will structurally characterize the conformational changes that occur when the lid opens, how oxidation affects the open and closed forms of the protein, and protein bound to inhibitors that may block mycobacterial infection and persistence. These studies will provide a greater mechanistic understanding of Mtb PTPs and their role in interfering with host signaling. The protein constructs used in these studies will include wild-type, wild-type oxidized, lid opening mutants, lid opening mutants-oxidized, and deleted lid protein with and without inhibitor.
该子项目是利用
由NIH/NCRR资助的中心赠款提供的资源。子项目和
研究者(PI)可能从另一个NIH来源获得了主要资金,
因此可以在其他CRISP条目中表示。所列机构为
研究中心,而研究中心不一定是研究者所在的机构。
酪氨酸磷酸化是一个重要的信号,它紧密调节免疫系统介导的许多细胞反应。 蛋白酪氨酸磷酸酶(PTP)通过其固有的去磷酸化活性拮抗这些关键的信号转导途径。 细胞内病原体,如结核分枝杆菌(Mtb),可以分泌PTP逃避宿主反应或实现免疫逃逸。 两种结核分枝杆菌PTP(PtpA和PtpB)的催化机制,细胞功能和宿主底物在很大程度上是未知的。 我会调查PtpB的自抑制盖,一种结构特征,阻止潜在的底物以及活性氧(ROS)进入蛋白质的活性位点。 我将从结构上描述盖子打开时发生的构象变化,氧化如何影响蛋白质的开放和封闭形式,以及与可能阻止分枝杆菌感染和持久性的抑制剂结合的蛋白质。 这些研究将提供一个更大的机制Mtb PTPs及其在干扰宿主信号传导的作用的理解。 在这些研究中使用的蛋白质构建体将包括野生型、野生型氧化、开盖突变体、开盖突变体-氧化和缺失的盖蛋白,有和没有抑制剂。
项目成果
期刊论文数量(0)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
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Elizabeth M Flynn其他文献
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{{ truncateString('Elizabeth M Flynn', 18)}}的其他基金
MECHANISTIC INSIGHTS INTO THE REGULATION OF AN MTB PROTEIN TYROSINE PHOSPHATASE
MTB 蛋白酪氨酸磷酸酶调节机制的见解
- 批准号:
7954317 - 财政年份:2009
- 资助金额:
$ 0.02万 - 项目类别:
MECHANISTIC INSIGHTS INTO THE REGULATION OF AN MTB PROTEIN TYROSINE PHOSPHATASE
MTB 蛋白酪氨酸磷酸酶调节机制的见解
- 批准号:
7721969 - 财政年份:2008
- 资助金额:
$ 0.02万 - 项目类别:
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