Premium
Branches on the α‐C Atom of Cyclosporin A Residue 3 Result in Direct Calcineurin Inhibition and Rapid Cyclophilin 18 Binding
Author(s) -
Zhang Yixin,
Raumgrass Ria,
Schutkowski Mike,
Fischer Gunter
Publication year - 2004
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200400020
Subject(s) - cyclophilin , calcineurin , cyclophilin a , chemistry , residue (chemistry) , fkbp , phosphatase , cyclosporins , peptidylprolyl isomerase , biochemistry , plasma protein binding , enzyme , stereochemistry , biology , microbiology and biotechnology , transplantation , isomerase , medicine , gene
It no longer takes two . We report on cyclosporin A (CsA) derivatives that inhibit calcineurin protein phosphatase activity without first forming a binary complex with cyclophilin 18. Furthermore, these derivatives are rapid binding inhibitors for cyclophilin 18, whereas CsA is a slow binding inhibitor.