THE AFFINITY OF THE EXCISED BINDING DOMAIN OF FK-506 FOR THE IMMUNOPHILIN FKBP12

Authors
TEAGUE SJ STOCKS MJ
Citation
Sj. Teague et Mj. Stocks, THE AFFINITY OF THE EXCISED BINDING DOMAIN OF FK-506 FOR THE IMMUNOPHILIN FKBP12, Bioorganic & medicinal chemistry letters, 3(10), 1993, pp. 1947-1950
Citations number
23
Categorie Soggetti
Chemistry Inorganic & Nuclear","Chemistry Medicinal
Journal title
Bioorganic & medicinal chemistry letters → ACNP
ISSN journal
0960894X
Volume
3
Issue
10
Year of publication
1993
Pages
1947 - 1950
Database
ISI
SICI code
0960-894X(1993)3:10<1947:TAOTEB>2.0.ZU;2-D
Abstract
The affinity of the binding domain of FK-506 was determined, in the ab sence of the constraints imposed upon it by the macrocyclic framework. Removal of those parts of FK-506 not involved in the binding of FK-50 6 to FKBP12 results in a 50-fold drop in affinity.