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Digitale Medien

Structural studies on FK-506, cyclosporin A and their immunophilin complexes (1994)

Clardy, Jon

Springer

Perspectives in drug discovery and design 2 (1994), S. 127-144

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Details

ISSN: 1573-9023

Schlagwort(e): Immunophilin ; FK-506 binding protein ; FKBP ; Cyclophilin ; X-ray structure ; Active site-ligand interactions ; Calcineurin

Quelle: Springer Online Journal Archives 1860-2000

Thema: Chemie und Pharmazie

Notizen: Summary The immunosuppressants FK-506 and cyclosporin A (CsA), along with their macromolecular receptors FKBP12 and cyclophilin A (CyPA), have become important targets for structure-based drug design. In the last few years X-ray diffraction and NMR spectroscopy have combined to provide high-resolution structures of FK-506, CyA, FKBP12, CyPA, FKBP12-FK-506, CyPA-CyA, and other complexes. This review summarizes these structural studies and some of their implications. Because the immunosuppressant-immunophilin complex forms a composite binding surface that interacts with yet another protein, structure-based drug design in this area is unusually challenging.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/BF02171740

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