Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant complex.
Science
; 252(5007): 839-42, 1991 May 10.
Article
en En
| MEDLINE
| ID: mdl-1709302
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.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Proteínas Portadoras
/
Inmunosupresores
/
Antibacterianos
Límite:
Humans
Idioma:
En
Revista:
Science
Año:
1991
Tipo del documento:
Article