Structure-based design of novel calcineurin (PP2B) inhibitors

The design, synthesis, and evaluation of small molecule, in vitro, inhibitors of human calcineurin is described. These ligands were derived from the known nonspecific phosphatase inhibitor endothall, and were modified to enhance binding and selectivity toward calcineurin using protein crystal struct...

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Bibliographic Details
Published inBioorganic & medicinal chemistry letters Vol. 7; no. 8; pp. 1007 - 1012
Main Authors Tatlock, John H., Angelica Linton, M., Hou, Xinjun J., Kissinger, Charles R., Pelletier, Laura A., Showalter, Richard E., Tempczyk, Anna, Ernest Villafranca, J.
Format Journal Article
LanguageEnglish
Published Oxford Elsevier Ltd 22.04.1997
Elsevier
Subjects
Biological and medical sciences
Immunomodulators
Medical sciences
Pharmacology. Drug treatments
Human
Cyclopropane derivatives
Enzyme
Phosphoprotein phosphatase
Phosphoric monoester hydrolases
Esterases
Organic anhydride
Tricyclic compound
Oxygen heterocycle
In vitro
Modeling
Immunomodulator
Structure activity relation
Molecular model
Hydrolases
Inhibitor
Immunosuppressive agent
Chemical synthesis
Acylate
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Summary:The design, synthesis, and evaluation of small molecule, in vitro, inhibitors of human calcineurin is described. These ligands were derived from the known nonspecific phosphatase inhibitor endothall, and were modified to enhance binding and selectivity toward calcineurin using protein crystal structure information. The design, synthesis and evaluation of small molecule inhibitors of human calcineurin is described. These ligands were derived from the known nonspecific phosphatase inhibitor endothall, and were modified to enhance binding and selectivity toward calcineurin using protein crystal structure information.
ISSN:0960-894X
1464-3405
DOI:10.1016/S0960-894X(97)00141-8