CRYSTAL STRUCTURES OF ION CHANNEL, SERPIN COMPLEXES, INTEGRON CARGO, MOLECULAR C

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 CLIC蛋白构成了一类新的氯离子通道蛋白，它以可溶性和整体膜的形式存在。我们已经解决了四种CLIC蛋白的结构，它们是CLIC1的可溶性形式和结构不同的膜对接形式。我们的目标是确定完整的膜形式以及蛋白质复合体的结构。Sm/LSM蛋白是许多RNPs(包括剪接体、端粒酶和降解体)的基础。我们已经解决了三个均质Sm/LSM环配合物，目前我们正在研究杂七聚体LSM结构以及RNP配合物。隐芽植物有一种独特的采光系统。我们解决了PE545在0.97？分辨率和PC645在1.4？分辨率的结构。这些50kD蛋白质中的每一个都与分辨率高得多的PE545 0.86和PC645发生了衍射波

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 four 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