ISSN:
1573-9023
Keywords:
Immunophilin
;
FK-506 binding protein
;
FKBP
;
Cyclophilin
;
X-ray structure
;
Active site-ligand interactions
;
Calcineurin
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF02171740
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