Structural Studies of Molecular Recognition by Proteins : X-ray Analyses of Complex Crystals

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Crystal structures of three transcription factor/DNA complexes, PHO4/DNA, IRF-2/DNA and Pap1/DNA, were determined. Based on these structures, molecular mechanisms of base recognition by these proteins were elucidated. In the mammalian signaling pathways, crystal structures of the small G protein RhoA in the GTPγS-MgィイD12+ィエD1 bound from and its complex with the effector protein PKN were determined. The structures reveals Rho-specific switching mechanisms and its recognition of the effector protein. Moreover, crystal structures of the thioredoxin-peroxidase HBP23 and a hippocampal serine protease, neuropsin, were determined. In the bacterial His-Asp phosphorelay signaling pathways, crystal structures of the HPt domain of a sensor kinase ArcB and its protein phosphatase SixA were determined.