VIRAL PROTEASE VP4

这个子项目是利用由NIH/NCRR资助的中心拨款提供的资源的许多研究子项目之一。子项目和调查员(PI)可能从另一个NIH来源获得了主要资金，因此可能会出现在其他CRISE条目中。列出的机构是针对中心的，而不一定是针对调查员的机构。我们正在研究一种新型病毒蛋白水解酶。这种酶是一种自我处理的类型，它在N-端和C-端裂解自己。它有一种独特的活性部位，在其他任何一组病毒蛋白酶中都找不到。我们的目标是解决这种病毒蛋白水解酶的结构，以便深入了解其机制的细节。此外，考虑到病毒感染养殖的鱼类，这些蛋白酶是潜在的药物靶标。我们得到了属于P6122空间群的酶的硒-蛋氨酸晶体。这些晶体的本源衍射率高于2.5A。我们也有P6122的天然晶体，在原点衍射率为2a。此外，我们还发现了同一种蛋白水解酶的三斜硒晶体。解决该结构的策略是MAD/SAD解决方案。我们希望，这些方法之一将使我们能够解决这些病毒蛋白水解酶的结构。如果可能，我们还包括两个更大的自然晶体(P6122)，以获得高分辨率的数据集。

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. We are studying a novel viral protease. This protease is a self-processing type, and it cleaves itself at its N- and C- terminus. It has a unique type of active site, not found in any other group of viral proteases. Our goal is to solve the structure of such viral protease, in order to gain insights into the details of its mechanisms. In addition, these proteases are potential drug targets, considering that the virus infects farmed fish. We have Seleno-Met crystals of the protease, that belong to space group P6122. These crystals diffract to better than 2.5A at the home source. We also have native crystals of P6122, that diffract to 2A at the home source. in addition we have some Seleno-Met triclinic crystals of the same protease. The strategy for solving the structure is a MAD / SAD solution. We hope that one of these approaches will allow us to solve the structure of these viral proteases. We are also including 2 larger native crystals (P6122) for a high resolution data set, if possible.