The crystal structure of unphosphorylated p38 MAP kinase complexed with a representative pyrrolotriazine-based inhibitor led to the elucidation of the high-affinity binding mode of this class of compounds at the ATP-binding site. The ligand binds in an extended conformation, with one end interacting
โฆ LIBER โฆ
Structural basis for the cyclophilin A binding affinity and immunosuppressive potency of E-ISA247 (voclosporin)
โ Scribed by Kuglstatter, Andreas ;Mueller, Francis ;Kusznir, Eric ;Gsell, Bernard ;Stihle, Martine ;Thoma, Ralf ;Benz, Joerg ;Aspeslet, Launa ;Freitag, Derrick ;Hennig, Michael
- Publisher
- International Union of Crystallography
- Year
- 2011
- Tongue
- English
- Weight
- 469 KB
- Volume
- 67
- Category
- Article
- ISSN
- 0907-4449
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โฆ Synopsis
X-ray crystal structures of the cyclosporin A analogue E-ISA247 (voclosporin) and its stereoisomer Z-ISA247 bound to cyclophilin A suggest the molecular basis for the differences in their binding affinities and immunosuppressive efficacies.
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