title: X-ray crystallography and NMR as tools for the study of protein tyrosine phosphatases.
abstract: Protein tyrosine phosphatases (PTPs) are well recognized as key targets in a wide spectrum of diseases, such as diabetes, obesity and cancer. Their roles in these maladies have been successfully characterized by various methods. However, it is only by utilizing the entire gamut of tools and techniques available that we can build a sufficient knowledge of their mode of action to bridge the gap between bench work and bedside treatments. Here, we highlight X-ray crystallography and NMR for the study of PTPs and describe methodological aspects of their use. These techniques are highly developed, versatile methods that together afford insight into protein dynamics, function and three-dimensional structure. They provide the detail necessary for the structure-based design and identification of lead compounds with potential as PTP-specific drugs for therapeutic use.
authors.affiliation: Department of Biochemistry and Groupe de recherche axé sur la structure des protéines, McGill University, 3649 Promenade Sir-William-Osler, Montreal, QC H3G 0B1, Canada.
authors.forename: Irina Elena
authors.initials: IE
authors.lastname: Gulerez
authors.affiliation: Department of Biochemistry and Groupe de recherche axé sur la structure des protéines, McGill University, 3649 Promenade Sir-William-Osler, Montreal, QC H3G 0B1, Canada. Electronic address: kalle.gehring@mcgill.ca.
authors.forename: Kalle
authors.initials: K
authors.lastname: Gehring
mesh_terms: D018360:Crystallography, X-Ray; D015195:Drug Design; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D017027:Protein Tyrosine Phosphatases / Q000737:chemistry*
chemical_list: D017027:Protein Tyrosine Phosphatases
keywords: Biophysics; Catalysis; NMR spectroscopy; Protein phosphatase; Structural biology; X-ray crystallography