CRYSTAL STRUCTURES OF ION CHANNEL, SERPIN COMPLEXES, AND OTHERS

Stanford University, Stanford CA

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Abstract

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 [unreadable] resolution and PC645 at 1.4 [unreadable] resolution. Each of these 50kD proteins diffract to much higher resolution PE545 0.86[unreadable] &PC645