MODELING THE STRUCTURE & DYNAMICS OF ACH ESTERASE CLUSTERS

结构建模

• 批准号: 7955236
• 负责人: PALMER William TAYLOR
• 金额: $ 0.32万
• 依托单位: UNIVERSITY OF CALIFORNIA, SAN DIEGO
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-05-01 至 2010-04-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7955236
• 关键词: Acetylcholine; Acetylcholinesterase; Biomedical Computing; Computer Retrieval of Information on Scientific Projects Database; Enzymes; Funding; Grant; Institution; Lead; Modeling; Neuromuscular Junction; Neurotransmitters; Research; Research Personnel; Resources; Signal Transduction; Source; Structure; Synapses; Synaptic Cleft; United States National Institutes of Health; Work; cholinergic synapse; esterase; monomer

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. This project investigates the consequences of the supramolecular structure of acetylcholinesterase (AChE) in the neuromuscular junction and other nicotinic cholinergic synapses. AChE must work extremely rapidly to clear the neurotransmitter acetylcholine (ACh) from such synapses after intercellular signaling has occurred. The AChE is organized into tetramers in the synaptic cleft, and in principle this could lead to inefficiencies if the monomers of enzyme compete strongly for ACh, since each monomer could effectively be "starved" for substrate.

这个子项目是许多研究子项目中的一个 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。 本计画探讨乙酰胆碱酯酶（AChE）在神经肌肉接头及其他烟碱型胆碱能突触中的超分子结构。 在细胞间信号传导发生后，乙酰胆碱酯酶必须非常迅速地工作以清除突触中的神经递质乙酰胆碱（ACh）。 乙酰胆碱酯酶在突触间隙中被组织成四聚体，原则上，如果酶的单体强烈竞争乙酰胆碱，这可能导致效率低下，因为每个单体可能有效地“饥饿”底物。