title: X-ray crystal structure of sangivamycin, a potent inhibitor of protein kinases.
abstract: The X-ray crystal structure of sangivamycin, a potent nucleoside inhibitor of protein kinases, has been determined. Sangivamycin crystallizes from water with its purine ring in a conformation anti to its ribose sugar. Such an anti conformation has been detected in solution for sangivamycin and other potent protein kinase inhibitors and appears to correlate with inhibitor potency [(1990) Biochemistry (in press)]. An intramolecular hydrogen bond between purine ring substituents is detected in the X-ray structure and may be an important structural feature of sangivamycin related to its degree of inhibition of rhodopsin kinase and of protein kinases C and A.
authors.affiliation: Department of Chemistry, University of South Carolina, Columbia 29208.
authors.forename: L
authors.initials: L
authors.lastname: Lebioda
authors.forename: P A
authors.initials: PA
authors.lastname: Hargrave
authors.forename: K
authors.initials: K
authors.lastname: Palczewski
mesh_terms: D003461:Crystallography; D006860:Hydrogen Bonding; D047428:Protein Kinase Inhibitors; D011741:Pyrimidine Nucleosides; D014867:Water; D014961:X-Ray Diffraction
chemical_list: D047428:Protein Kinase Inhibitors; D011741:Pyrimidine Nucleosides; D014867:Water; C005699:sangivamycin