XRAY CRYSTALLOGRAPHIC STUDY OF CYTOPLASMIC DOMAIN OF SERINE CHEMORECEPTOR

$143,176P41FY2002RRNIH

Stanford University, Stanford CA

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Abstract

This research will address the question of signaling mechanisms at molecular level by determining the X-ray crystallographic structure of the cytoplasmic domain of a chemoreceptor from E. coli and its mutant which shows different signaling behavior. The structure determination of cytoplasmic domain of wild type serine receptor and its mutant with different methylation states will give us the information on signal transfer and adaptation mechanism through membrane receptor.

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