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1fap
From Proteopedia
THE STRUCTURE OF THE IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-RAPAMYCIN COMPLEX INTERACTING WITH HUMAN FRAP
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.
Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP., Choi J, Chen J, Schreiber SL, Clardy J, Science. 1996 Jul 12;273(5272):239-42. PMID:8662507
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1FAP is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Choi J, Chen J, Schreiber SL, Clardy J. Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP. Science. 1996 Jul 12;273(5272):239-42. PMID:8662507
Page seeded by OCA on Tue Feb 17 07:56:45 2009
