X‐ray crystal structure of sangivamycin, a potent inhibitor of protein kinases

FEBS Letters

Palczewski, Krzysztof¹  Hargrave, Paul A²  Lebioda, Lukasz³ 

[1] Department of Ophthalmology, Robert S. Dow Neurological Sciences Institute, Good Samaritan Hospital and Medical Center, Portland, OR 97209-1595, USA;Department of Ophthalmology, and Department of Biochemistry and Molecular Biology, University of Florida, Gainesville, FL 32610 USA;Department of Chemistry, University of South Carolina, Columbia, SC 29208, USA

关键词: Inhibitor;    Protein kinase;    Nucleoside;    sangivamycin;    4-amino-5-carboxamide-7(β-D-ribofuranosyl)pyrrolo[2;    3-d]-pyrimidine;   

DOI  :  10.1016/0014-5793(90)81517-R

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown