Journal of the American Chemical Society p. 9925 - 9938 (1993)
Update date:2022-08-03
Topics:
Holt, Dennis A.
Luengo, Juan I.
Yamashita, Dennis S.
Oh, Hye-Ja
Konialian, Arda L.
Yen, Hwa-Kwo
Rozamus, Leonard W.
Brandt, Martin
Bossard, Mary J.
Levy, Mark A.
Eggleston, Drake S.
Liang, Jun
Wayne Schultz
Stout, Thomas J.
Clardy, Jon
The design and synthesis of high-affinity FKBP12 ligands is described. These compounds potently inhibit the cis-trans-peptidylprolyl isomerase (rotamase) activity catalyzed by FKBP12 with inhibition constants (Ki,app) as low as 1 nM, yet they possess remarkable structural simplicity relative to FK506 and rapamycin, from which they are conceptually derived. The atomic structures of three FKBP12-ligand complexes and of one unbound ligand were determined by X-ray crystallography and are compared to the FKBP12-FK506 and FKBP12-rapamycin complexes.
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Doi:10.1021/jo961012z
(1996)Doi:10.1016/S0957-4166(00)80420-6
(1993)Doi:10.1016/0223-5234(93)90096-W
(1993)Doi:10.1016/0022-328X(93)80359-J
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(1979)
