Main Body
Investigators and Program Directors
Patrick Van Roey
Research Scientist, Wadsworth Center,
Computational & Structural Biology
Associate Professor, School of Public Health, Biomedical Sciences
Ph.D., University of Calgary, Calgary, Alberta, Canada
(1979)
Postdoctoral training, Medical Foundation of Buffalo
Research Interests
The research activities of our laboratory involve the determination of the three-dimensional structures of macromolecules by X-ray crystallography with an emphasis on the analysis of intermolecular interactions as they relate to substrate and ligand recognition. Ongoing projects include:
- Protein-carbohydrate interactions in enzymes that release oligosaccharides from glycoproteins, including glycohydrolases and glycoamidases. Current emphasis is on the analysis of the substrate specificity of endoglycosidases and peptide-N-glycanases. These enzymes are used as biochemical tools for the analysis of oligosaccharides and the deglycosylation of proteins for structural analysis. The endoglycosidases under investigation have identical mechanisms but specificities for distinct forms of N-linked glycans. The glycanases process the similar substrates but differ in structure as well as in catalytic mechanism.
- Mechanisms of action and substrate recognition of intron-encoded endonucleases. We are studying the structures of I-TevI and I-DmoI, representatives of two distinct families of homing endonucleases. These enzymes catalyze double-strand DNA cleavage to initiate mobility of their introns. The two enzymes interact with lengthy DNA sequences and have high cleavage site specificities. Crystallographic studies of the enzymes and their complexes with DNA substrates will allow determination of the mechanism of action and DNA recognition.
- Glycohormone-receptor interaction. Follicle stimulating hormone (FSH) is a member of the family of pituitary glycohormones that bind to membrane bound G protein coupled receptors. The FSH-receptor interaction is important in fertility. Crystallographic studies of human FSH and of the extra cellular domain of its receptor will lead to the identification of residues involved in hormone-receptor binding and allow analysis of the relationship between receptor-binding and signal transduction.
Contact Information
E-mail: vanroey@wadsworth.org.
