VIRAL PROTEASE VP4

本子项目是利用由NIH/NCRR资助的中心赠款提供的资源的众多研究子项目之一。子项目和研究者（PI）可能已经从另一个NIH来源获得了主要资金，因此可以在其他CRISP条目中表示。列出的机构是中心的，不一定是研究者的机构。我们正在研究一种新的病毒蛋白酶。这种蛋白酶是一种自我加工型蛋白酶，它在N端和C端切割自己。它有一种独特的活性位点，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酶的结构，以便深入了解其机制的细节。此外，考虑到该病毒感染养殖鱼类，这些蛋白酶是潜在的药物靶点。我们有蛋白酶的硒- met晶体，属于P6122空间群。这些晶体在主光源处的衍射优于2.5A。我们也有P6122的原生晶体，在主光源处衍射到2A。此外，我们有一些相同蛋白酶的硒- met三斜晶体。解决该结构的策略是一个MAD / SAD解决方案。我们希望这些方法中的一种将使我们能够解决这些病毒蛋白酶的结构。如果可能的话，我们还包括2个较大的天然晶体（P6122），用于高分辨率数据集。

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.