MODELING THE STRUCTURE & DYNAMICS OF ACH ESTERASE CLUSTERS

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 本项目研究神经肌肉接头和其他烟碱型胆碱能突触中乙酰胆碱酯酶(AChE)的超分子结构的后果。在细胞间信号传递发生后，AChE必须非常迅速地从这些突触中清除神经递质乙酰胆碱(ACh)。AChE在突触裂隙中被组织成四个异构体，原则上，如果酶的单体强烈竞争ACh，这可能会导致效率低下，因为每个单体都可能有效地“饥饿”底物。

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.