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Structure of the FKBP12-Rapamycin Complex Interacting with the Binding Domain of Human FRAP

Choi, Jungwon ; Chen, Jie ; Schreiber, Stuart L. ; Clardy, Jon

Science (American Association for the Advancement of Science), 1996-07, Vol.273 (5272), p.239-242 [Periódico revisado por pares]

Washington, DC: American Society for the Advancement of Science

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Título:
Structure of the FKBP12-Rapamycin Complex Interacting with the Binding Domain of Human FRAP
Autor: Choi, Jungwon ; Chen, Jie ; Schreiber, Stuart L. ; Clardy, Jon
Assuntos: Analytical, structural and metabolic biochemistry ; Atomic interactions ; Atoms ; Binding and carrier proteins ; Binding Sites ; Biochemistry ; Biological and medical sciences ; Carrier proteins ; Carrier Proteins - chemistry ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Cell cycle ; Complex compounds ; Coordination compounds ; Crystallography, X-Ray ; Dimerization ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - metabolism ; Electron density ; Electronic structure ; FK 506 ; Fundamental and applied biological sciences. Psychology ; Heat-Shock Proteins - chemistry ; Heat-Shock Proteins - metabolism ; Humans ; Hydrogen bonds ; Immunophilins ; Immunosuppressive agents ; Ligands ; Models, Molecular ; Molecular biology ; Molecules ; Mutation ; Phosphotransferases (Alcohol Group Acceptor) ; Polyenes - chemistry ; Polyenes - metabolism ; Protein Conformation ; Protein structure ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proteins ; Recombinant Proteins - chemistry ; Recombinant Proteins - metabolism ; Sirolimus ; Structure ; Surface areas ; Tacrolimus Binding Proteins ; TOR Serine-Threonine Kinases ; Transport proteins
É parte de: Science (American Association for the Advancement of Science), 1996-07, Vol.273 (5272), p.239-242
Notas: ObjectType-Article-2
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Descrição: Rapamycin, a potent immunosuppressive agent, binds two proteins: the FK506-binding protein (FKBP12) and the FKBP-rapamycin-associated protein (FRAP). A crystal structure of the ternary complex of human FKBP12, rapamycin, and the FKBP12-rapamycin-binding (FRB) domain of human FRAP at a resolution of 2.7 angstroms revealed the two proteins bound together as a result of the ability of rapamycin to occupy two different hydrophobic binding pockets simultaneously. The structure shows extensive interactions between rapamycin and both proteins, but fewer interactions between the proteins. The structure of the FRB domain of FRAP clarifies both rapamycin-independent and -dependent effects observed for mutants of FRAP and its homologs in the family of proteins related to the ataxia-telangiectasia mutant gene product, and it illustrates how a small cell-permeable molecule can mediate protein dimerization.
Editor: Washington, DC: American Society for the Advancement of Science
Idioma: Inglês

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Structure of the FKBP12-Rapamycin Complex Interacting with the Binding Domain of Human FRAP

Choi, Jungwon ; Chen, Jie ; Schreiber, Stuart L. ; Clardy, Jon

Washington, DC: American Society for the Advancement of Science

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