CRYSTALLOGRAPHIC STUDIES ON NUCLEAR PORE COMPLEX PROTEINS

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。 核孔复合物（nuclear pore complex，NPC）是真核细胞中最大的蛋白质组装体，介导核质间的转运。NPC有大约30种独特的蛋白质（称为核孔蛋白），在脊椎动物中聚集在一起形成大约125 MDa的蛋白质复合物。尽管它在真核细胞生理学中的重要作用，NPC组织的结构细节及其在核运输中的作用尚未建立。因此，对NPC的结构研究是重要的，以阐明组装的NPC及其在各种生理过程中的作用，如mRNA输出，病毒进入细胞核，运输癌症相关因子等。我们的长期目标是重建脊椎动物NPC的各种子复合物，并进行晶体学研究，以确定高分辨率的三维结构。

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 nuclear pore complex (NPC) is the largest protein assembly in eukaryotic cell, which mediate transport between nucleus and cytoplasm. NPC have approximately 30 unique proteins (known as nucleoporins), clustered together to form approximately 125 MDa protein complex in vertebrates. In spite of its important role in eukaryotic cell physiology, the structural details of NPC organization and its role in nuclear transport are not established yet. Structural studies on NPC are therefore important to elucidate the assembly of NPC and its role in various physiological processes such as mRNA export, viral entry into the nucleus, transport of cancer related factors etc. Our long-term goal is to reconstitute various sub complexes of vertebrate NPC and undertake crystallographic studies to determine high-resolution 3D structure.