The affinity of the excised binding domain of FK-506 for the immunophilin FKBP12

The affinity of the binding domain of FK-506 was determined, in the absence of the constraints imposed upon it by the macrocyclic framework. Removal of those parts of FK-506 not involved in the binding of FK-506 to FKBP12 results in a 50-fold drop in affinity. The affinity of the FK-506 binding doma...

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Bibliographic Details
Published in:Bioorganic & medicinal chemistry letters 1993-10, Vol.3 (10), p.1947-1950
Main Authors: Teague, Simon J., Stocks, Michael J.
Format: Article
Language:English
Subjects:
Biological and medical sciences
Immunomodulators
Medical sciences
Pharmacology. Drug treatments
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Summary:The affinity of the binding domain of FK-506 was determined, in the absence of the constraints imposed upon it by the macrocyclic framework. Removal of those parts of FK-506 not involved in the binding of FK-506 to FKBP12 results in a 50-fold drop in affinity. The affinity of the FK-506 binding domain, in the absence of the constraints imposed upon it by the macrocyclic framework, is reported.
ISSN:0960-894X
1464-3405
DOI:10.1016/S0960-894X(01)80992-6