POTENTIAL CRYSTAL GROWTH Of Clostridium perfringens LARGE NanH IN SPACE AS TARGETS FOR DRUG DESIGN

摘要

X-ray diffraction analysis elucidates the atomic structure of a protein for providing a basis of drug designs. Neuraminidase, NanH, have been found in many pathogenic microorganisms and involved in the mechanisms of invasion into mammalian cells. We have cloned large nanH gene of a pathogenic bacteria Clostridium perfringens, which grow in anaerobic condition and cause many diseases in human and animals. It is very important to find the inhibitors of NanH to hinder the infections of bacteria ; X-ray crystallography is a powerful method to assess this problem. The three dimentional structure of C. perfringens NanH (73 kDa) has been partially resolved by computor modeling techniques with virus NanH as the parent structure. Site-directed mutagenesis analysis indicated that Glu 539 are found to be involved in the catalytic activity of large NanH. We anticipate that three dimentional structure of space-grown crystals with resolution less than 2A will provide better implications for the spatial arrangement of the catalytic residues and inhibitors of the enzyme-inhibitor complex.