91057-85-1Relevant academic research and scientific papers
Design, synthesis, and kinetic evaluation of high-affinity FKBP ligands and the X-ray crystal structures of their complexes with FKBP 12
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
, p. 9925 - 9938 (2007/10/02)
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.
