CRYSTAL STRUCTURES OF ION CHANNEL, SERPIN COMPLEXES, AND OTHERS

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。 CLIC蛋白构成了一类新的氯离子通道蛋白，其以可溶性和完整膜形式存在。 我们已经解决了五个CLIC蛋白质的可溶性形式和CLIC 1的结构不同的膜对接形式的结构。 我们的目标是确定完整的膜形式以及蛋白质复合物的结构。 Sm/Lsm蛋白形成许多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质Sm/LSM环配合物，我们目前正在研究杂七聚LSM结构以及RNP配合物。 隐藻有独特的捕光系统。 我们已经解决了PE 545在0.97分辨率和PC 645在1.4分辨率的结构。 这些50 kD蛋白质中的每一个都能以高得多的分辨率PE 545 0.86 <$& 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