CRYSTAL STRUCTURES OF ION CHANNEL, SERPIN COMPLEXES, AND OTHERS

该子项目是利用该技术的众多研究子项目之一 资源由 NIH/NCRR 资助的中心拨款提供。子项目及 研究者 (PI) 可能已从 NIH 的另一个来源获得主要资金， 因此可以在其他 CRISP 条目中表示。列出的机构是 对于中心来说，它不一定是研究者的机构。 CLIC蛋白构成一类新的氯离子通道蛋白，其以可溶性和完整膜形式存在。 我们已经解析了五种可溶形式的 CLIC 蛋白的结构以及结构上不同的 CLIC1 膜对接形式。 我们的目标是确定完整膜形式以及蛋白质复合物的结构。 Sm/Lsm 蛋白构成了许多 RNP（包括剪接体、端粒酶和降解体）的基础。我们已经解决了三个同聚 Sm/Lsm 环复合物，目前正在研究异七聚 Lsm 结构以及 RNP 复合物。 隐植物具有独特的光收集系统。 我们已经解析了 0.97 ¡ 分辨率的 PE545 和 1.4 ¡ 分辨率的 PC645 的结构。 这些 50kD 蛋白质中的每一个都可衍射至更高分辨率的 PE545 0.86¿ 和 PC645

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 CLIC proteins constitute a new class of chloride ion channel proteins which exist in both a soluble and integral membrane forms. We have solved the structures of five CLIC proteins in the soluble form and a structurally distinct membrane docking form of CLIC1. We aim is to determine the structure of the integral membrane form as well as protein complexes. The Sm/Lsm proteins form the basis for many RNPs (including the spliceosome, telomerase and degradosome). We have solved three homomeric Sm/Lsm ring complexes and we are currently working on heteroheptameric Lsm structures as well as RNP complexes. Cryptophytes have a unique light harvesting system. We have solved the structures of PE545 at 0.97 ¿ resolution and PC645 at 1.4 ¿ resolution. Each of these 50kD proteins diffract to much higher resolution PE545 0.86¿ & PC645