CALMODULIN TARGET PROTEINS; STRUCTURE-FUNCTION RELATIONSHIPS

钙调蛋白靶蛋白；

• 批准号: 7601295
• 负责人: ALLEN R RHOADS
• 金额: $ 0.03万
• 依托单位: CARNEGIE-MELLON UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2007
• 资助国家: 美国
• 起止时间: 2007-08-01 至 2008-07-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7601295
• 关键词: ATP phosphohydrolase; Adenylate Cyclase; Affinity; Age; Amino Acid Motifs; Amino Acid Sequence; Binding; Binding Proteins; Binding Sites; Bordetella pertussis; Calcineurin; Calcium; Calmodulin; Class; Computer Retrieval of Information on Scientific Projects Database; Databases; EF Hand Motifs; Enzymes; Evolution; Family; Funding; Genes; Genome; Glycogen Phosphorylase; Grant; Growth Associated Protein 43; Institution; Lithium; Lung; Molecular; Myosin Light Chain Kinase; Nitric Oxide Synthase; Nucleotides; Peptide Sequence Determination; Phosphorylase Kinase; Phosphorylation Site; Phylogenetic Analysis; Positioning Attribute; Procedures; Protein Binding; Protein Dynamics; Proteins; Pseudogenes; Psychiatry; Publications; Pump; Radiation Hybrid Map; Radiation Hybrid Mapping; Relative (related person); Research; Research Personnel; Resources; Signal Pathway; Source; Structure; Structure-Activity Relationship; Taxon; Trace Elements; United States National Institutes of Health; calcium-dependent protein kinase; caldesmon; fodrin; macrophage; myristoylated alanine-rich C kinase substrate; neurogranin; phosphoric diester hydrolase; programs; protein structure function

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 research plan involves examining the different families of calmodulin-dependent proteins to determine: (1) structural or functional binding motifs of calmodulin(CAM) and the position of phosphorylation sites or pseudosubstrate domains or homologous regions relative to the CAM-binding domain; (2) comparison of EF-hand proteins in different eucaryotic genomes and tracing elements of their signaling pathways; (3) searching the database for sequences similar to regions associated with CAM binding and secondary structure prediction in the vicinity of the CAM-binding site; (4) examining the phylogenetic relationships and ages of divergence among taxa utilizing retroprocessed CAM pseudogenes as neutral markers of evolution (5) examination of local multiple alignments of CAM-binding proteins by dynamic programming procedures. Protein sequences investigated include the entire spectrum of CAM target proteins. The spectrum includes: Class 1 target proteins that bind to CAM without associated calcium and may have reduced affinity for calcium/CAM; Class 2 proteins that bind CAM strongly in the absence of calcium and may be positively activated by calcium; and the major Class 3 proteins that have high affinity for the calcium/CAM and are activated by it. Class 1 examples are neuromodulin, neurogranin and some IQ motif proteins. Class 2 are macrophage NO synthase, lung cyclic 3`, 5`-nucleotide phosphodiesterase, bordetella pertussis adenylate cyclase, and glycogen phosphorylase b kinase;and class 3 containing the enzymes and proteins such as calcineurin, myosin light chain kinase, caldesmon, adenylate cyclases, fodrin, MARCKS protein, adducins, protein kinases, calcium-dependent ATPase pumps and others. Publications - Rhoads, A.R. and Friedberg, F.: "Sequence Motifs for Calmodulin Recognition.": FASEB J. 11: 331-340: 1997; Rhoads, A.R., Karkera, J.D., and Detera-Wadleigh, S.D.: "Radiation Hybrid Mapping of Genes in the Lithium-Sensitive Wnt Signaling Pathway." : Molecular Psychiatry 4: 437-442: 1999; Friedberg, F. and Rhoads, A.R.: "Calculation and Verification of the Ages of Retroprocessed Pseudogenes.": Molecular Phylogenetics and Evolution: 16: 2000 (In Press);

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此可以在其他清晰的条目中代表。列出的机构是 对于中心，这不一定是调查员的机构。 该研究计划涉及检查钙调蛋白依赖性蛋白的不同家族以确定：（1）钙调蛋白（CAM）的结构或功能结合基序以及相对于凸轮结合域的磷酸化位点或磷酸化位点或假性底物域或同源区域的位置； （2）比较不同胞核基因组中的EF手蛋白和信号通路的追踪元素； （3）搜索数据库中的序列类似于与CAM结合和辅助结构预测相似的凸轮结合位点附近的序列； （4）检查分类群中的系统发育关系和差异的年龄，利用经过重新处理的CAM伪基因作为进化的中性标志物（5）通过动态编程程序检查局部多个凸轮结合蛋白的多重比对。研究的蛋白质序列包括CAM靶蛋白的全部光谱。频谱包括：1类靶蛋白，它们与CAM结合而无需钙，并且可能会降低对钙/CAM的亲和力；在不存在钙的情况下强烈结合CAM的2类蛋白质可以通过钙积极地激活；以及对钙/CAM具有高亲和力并被其激活的主要3类蛋白。第1类的例子是神经化蛋白，神经素蛋白和一些智商基序蛋白。 Class 2 are macrophage NO synthase, lung cyclic 3`, 5`-nucleotide phosphodiesterase, bordetella pertussis adenylate cyclase, and glycogen phosphorylase b kinase;and class 3 containing the enzymes and proteins such as calcineurin, myosin light chain kinase, caldesmon, adenylate cyclases, fodrin, MARCKS蛋白质，添加剂，蛋白激酶，依赖钙的ATPase泵等。 出版物 - Rhoads，A.R。弗里德伯格（Friedberg），f。：“钙调蛋白识别的序列主题。”：Faseb J. 11：331-340：1997； A.R. Rhoads，J.D。Karkera和S.D. Detera-Wadleigh：“对锂敏感的Wnt信号通路中基因的辐射杂交映射”。 ：分子精神病学4：437-442：1999;弗里德伯格（F.