MODELING THE STRUCTURE & DYNAMICS OF ACH ESTERASE CLUSTERS

结构建模

• 批准号: 7601688
• 负责人: PALMER William TAYLOR
• 金额: $ 0.18万
• 依托单位: UNIVERSITY OF CALIFORNIA, SAN DIEGO
• 依托单位国家: 美国
• 财政年份: 2007
• 资助国家: 美国
• 起止时间: 2007-05-01 至 2008-04-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7601688
• 关键词: Acetylcholine; Acetylcholinesterase; Chromosome Pairing; 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.

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。 该项目研究了神经肌肉连接和其他烟碱胆碱能突触中乙酰胆碱酯酶（ACHE）超分子结构的后果。 发生在细胞间信号后，ACHE必须非常快速地从此类突触中清除神经递质乙酰胆碱（ACH）。 在突触裂隙中，将ACHE组织到四聚体中，从原则上讲，如果酶的单体竞争激烈的ACH，这可能导致效率低下，因为每个单体都可以有效地“饿死”底物。