1FKF

ATOMIC STRUCTURE OF FKBP-FK506, AN IMMUNOPHILIN-IMMUNOSUPPRESSANT COMPLEX

Summary for 1FKF

• Entry DOI: 10.2210/pdb1fkf/pdb
• Descriptor: FK506 BINDING PROTEIN, 8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN (3 entities in total)
• Functional Keywords: isomerase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytosol : P62942
• Total number of polymer chains: 1
• Total formula weight: 12640.53

Authors

Vanduyne, G.D.,Standaert, R.F.,Karplus, P.A.,Schreiber, S.L.,Clardy, J. (deposition date: 1991-05-07, release date: 1991-07-15, Last modification date: 2024-02-07)

Primary citation

Van Duyne, G.D.,Standaert, R.F.,Karplus, P.A.,Schreiber, S.L.,Clardy, J.
Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant complex.
Science, 252:839-842, 1991

PubMed Abstract: The structure of the human FK506 binding protein (FKBP), complexed with the immunosuppressant FK506, has been determined to 1.7 angstroms resolution by x-ray crystallography. The conformation of the protein changes little upon complexation, but the conformation of FK506 is markedly different in the bound and unbound forms. The drug's association with the protein involves five hydrogen bonds, a hydrophobic binding pocket lined with conserved aromatic residues, and an unusual carbonyl binding pocket. The nature of this complex has implications for the mechanism of rotamase catalysis and for the biological actions of FK506 and rapamycin.

PubMed: 1709302

Experimental method

X-RAY DIFFRACTION (1.7 Å)