Proceedings of the Korean Biophysical Society Conference (한국생물물리학회:학술대회논문집)

The Korean Biophysical Society (한국생물물리학회)
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STRUCTURAL ANALYSIS OF RAPAMYCIN'S ROLE IN BINDING FKBP12 AND FRAP

  • Park, Jungwon (Department of Chemistry, University of Suwon) ;
  • Jie Chen (Howard Hughes Medical Institute, Department of Chemistry, Harvard University) ;
  • Stuart Schreiber (Howard Hughes Medical Institute, Department of Chemistry, Harvard University) ;
  • Jon Clardy (Department of Chemistry, Cornell University)
  • Published : 1996.07.01
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Abstract

The immunosuppressive and cell cycle arrest agent rapamycin works by binding together two proteins: the FK506 binding protein (FKBP12) and the FKBP-rapamycin associated protein (FRAP). A 2.7 $\AA$ resolution crystal structure of the triple complex of human FK506 binding protein (FKBP12), rapamycin, and FKBP12-rapamycin binding domain (FRB) of FRAP, reveals two proteins bound together through rapamycin' s ability to simultaneously occupy two different hydrophobic binding pockets. (omitted)

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