TY - JOUR
T1 - Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin
AU - Michnick, Stephen W.
AU - Rosen, Michael K.
AU - Wandless, Thomas J.
AU - Karplus, Martin
AU - Schreiber, Stuart L.
PY - 1991/5/10
Y1 - 1991/5/10
N2 - Immunophilins, when complexed to immunosuppressive ligands, appear to inhibit signal transduction pathways that result in exocytosis and transcription. The solution structure of one of these, the human FK506 and rapamycin binding protein (FKBP), has been determined by nuclear magnetic resonance (NMR). FKBP has a previously unobserved antiparallel β-sheet folding topology that results in a novel loop crossing and produces a large cavity lined by a conserved array of aromatic residues; this cavity serves as the rotamase active site and drug-binding pocket. There are other significant structural features (such as a protruding positively charged loop and an apparently flexible loop) that may be involved in the biological activity of FKBP.
AB - Immunophilins, when complexed to immunosuppressive ligands, appear to inhibit signal transduction pathways that result in exocytosis and transcription. The solution structure of one of these, the human FK506 and rapamycin binding protein (FKBP), has been determined by nuclear magnetic resonance (NMR). FKBP has a previously unobserved antiparallel β-sheet folding topology that results in a novel loop crossing and produces a large cavity lined by a conserved array of aromatic residues; this cavity serves as the rotamase active site and drug-binding pocket. There are other significant structural features (such as a protruding positively charged loop and an apparently flexible loop) that may be involved in the biological activity of FKBP.
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U2 - 10.1126/science.1709301
DO - 10.1126/science.1709301
M3 - Article
C2 - 1709301
AN - SCOPUS:0025826966
SN - 0036-8075
VL - 252
SP - 836
EP - 839
JO - Science
JF - Science
IS - 5007
ER -