X‐ray crystal structure of sangivamycin, a potent inhibitor of protein kinases
Open Access
- 18 June 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 266 (1-2) , 102-104
- https://doi.org/10.1016/0014-5793(90)81517-r
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.Keywords
This publication has 11 references indexed in Scilit:
- Regulatory Domain of Calcium/Calmodulin-dependent Protein Kinase IIPublished by Elsevier ,1989
- Purification and characterization of rhodopsin kinase.Journal of Biological Chemistry, 1988
- Autoregulation of Enzymes by Pseudosubstrate Prototopes: Myosin Light Chain KinaseScience, 1988
- K-252a, a novel microbial product, inhibits smooth muscle myosin light chain kinase.Journal of Biological Chemistry, 1988
- Sangivamycin, a nucleoside analogue, is a potent inhibitor of protein kinase C.Journal of Biological Chemistry, 1988
- A Fluorescent Protein Kinase C Inhibitor: 1-(1-Hydroxy-5-isoquinolinylsulfonyl)piperazinePharmacology, 1988
- Mapping of the adenosine 5'-triphosphate binding site of type II calmodulin-dependent protein kinaseBiochemistry, 1987
- Isoquinolinesulfonamides, novel and potent inhibitors of cyclic nucleotide-dependent protein kinase and protein kinase CBiochemistry, 1984
- ATP analog specificity of cAMP-dependent protein kinase, cGMP-dependent protein kinase, and phosphorylase kinaseEuropean Journal of Biochemistry, 1984
- Probing the interrelation between the glycosyl torsion, sugar pucker, and the backbone conformation in C(8) substituted adenine nucleotides by proton and proton-phosphorus-31 fast Fourier transfer nuclear magnetic resonance methods and conformational energy calculationsJournal of the American Chemical Society, 1974