CRYSTAL STRUCTURES OF ION CHANNEL, SERPIN COMPLEXES, AND OTHERS

这个子项目是许多利用资源的研究子项目之一 由NIH/NCRR资助的中心拨款提供。子项目的主要支持 而子项目的主要调查员可能是由其他来源提供的， 包括其它NIH来源。 列出的子项目总成本可能 代表子项目使用的中心基础设施的估计数量， 而不是由NCRR赠款提供给子项目或子项目工作人员的直接资金。 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. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. 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