1. X-ray crystallographic analyses of the gene V protein from Ff bacteriophage, a single-stranded DNA-binding protein, and its Y41 mutants 2. X-ray crystallographic analyses of several anticancer drugs and their interactions with DNA.

摘要

In biological systems, DNA/RNA-protein interactions as well as drug-DNA interactions play important roles in genetic processes. A fundamental understanding of these processes requires a detailed structural knowledge of DNAs, proteins, drugs, as well as their complexes with each other. Gene V protein (GVP) encoded by the filamentous bacteriophage Ff (M13, f1, fd) is a single-stranded DNA (ssDNA) binding protein which binds to ssDNA non-specifically and cooperatively. The structure of the wild-type protein has been determined and refined at 1.8A resolution (Skinner et al., (1994) Proc. Natl. Acad. Sci. USA. 91, 2071-2075). It is largely composed of ;Several drug molecules such as ecteinascidins and UK63052, are potent anticancer drugs. The high resolution crystal structural analyses as well as the modeling studies of these molecules provide us with valuable information on how these molecules exert their functions in the living cells. Cyclic ribodiguanylic acid, c-(GpGp), is the endogenous effector regulator of cellulose synthase. Their structural analyses help us in understanding the structure-function relationship of cyclic-DNA/RNAs.