This domain forms an alpha helical structure and binds to rapamycin (PMID:8662507).
Family alignment:
There are 2043 Rapamycin_bind domains in 2040 proteins in SMART's nrdb database.
Click on the following links for more information.
Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing Rapamycin_bind domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with Rapamycin_bind domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing Rapamycin_bind domain in the selected taxonomic class.
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP.
Science. 1996; 273: 239-42
Display abstract
Rapamycin, a potent immunosuppressive agent, binds two proteins: theFK506-binding protein (FKBP12) and the FKBP-rapamycin-associated protein (FRAP). A crystal structure of the ternary complex of human FKBP12, rapamycin, and theFKBP12-rapamycin-binding (FRB) domain of human FRAP at a resolution of 2.7angstroms revealed the two proteins bound together as a result of the ability of rapamycin to occupy two different hydrophobic binding pockets simultaneously. Thestructure shows extensive interactions between rapamycin and both proteins, butfewer 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 theataxia-telangiectasia mutant gene product, and it illustrates how a smallcell-permeable molecule can mediate protein dimerization.