STRUCTURAL STUDIES OF THE MOLECULAR CHAPERONES-HSP104/CLPB

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。 ClpB/Hsp 104是ATP依赖性分子伴侣，形成600 kDa的六聚体单环结构。我们已经解决了与AMPPNP结合的ClpB全长的晶体结构（Lee等人，为了解决底物识别的结构基础，我们现在已经结晶了全长ClpB-肽复合物，并希望使用X射线晶体学确定该复合物的结构。 除了其在耐热性中的作用之外，Hsp 104还需要用于[PSI+]的遗传和维持，[PSI+]是一种酵母朊病毒样元件，其类似于其哺乳动物对应物，其特征在于淀粉样纤维形成。我们希望确定Hsp 104的晶体结构，以研究Hsp 104在[PSI+]传播中的结构和功能。

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. ClpB/Hsp104 are ATP-dependent molecular chaperones and form hexameric, single ring structures of 600 kDa. We have solved the crystal structure of ClpB full-length bound to AMPPNP (Lee et al., 2003)To address the structural basis of substrate recognition, we have now crystallized a full-lenth ClpB-peptide complex and wish to determine the structure of this complex using x-ray crystallography. In addition to its role in thermotolerance, Hsp104 is also required for the inheritance and maintenance of [PSI+], a yeast prion-like element that, similar to its mammalian counterpart, is characterized by amyloid fiber formation. We wish to determine the crystal structure of Hsp104 to study the structure and function of Hsp104 in [PSI+] propagation.