TOWARD GAINING INSIGHTS INTO THE MECHANISM OF SUBSTRATE TRANSPORT BY THE ASPART

这个子项目是利用资源的许多研究子项目之一。 由NIH/NCRR资助的中心拨款提供。对子项目的主要支持 子项目的首席调查员可能是由其他来源提供的， 包括美国国立卫生研究院的其他来源。为子项目列出的总成本可能 表示该子项目使用的中心基础设施的估计数量， 不是由NCRR赠款提供给次级项目或次级项目工作人员的直接资金。 神经递质转运蛋白是一种膜蛋白，它利用钠的电化学梯度将其底物/神经递质从细胞外区域向上转移到细胞内部。这一过程涉及从外向构象到内向构象的结构转变，从而实现底物的循环识别/结合和释放。天冬氨酸转运蛋白GltPh是人类谷氨酸转运蛋白的古老同源物，其晶体结构在这两种构象中都已被解析。我们打算使用这两种晶体结构进行MD运行，以深入了解在这两种构象之间的通道中起驱动作用的分子相互作用机制。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Neurotransmitter transporters are membrane proteins that utilize the electrochemical gradient of sodium for uphill translocation of their substrate/neurotransmitter from the extracellular region to the cell interior. This process involves a structural transition from outward-facing conformation to inward-facing conformation that enables the cyclical recognition/binding and release of the substrate. The crystal structure of the aspartate transporter GltPh, an archaeal homologue of human glutamate transporters, has been resolved in both conformations. We intend to perform MD runs using these two crystal structures towards gaining insights into molecular mechanisms of interactions that play a driving role in the passage between these two conformers.