Oliver's mTOR Atlas Evidence Platform
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Pathway link RAPA-FKBP12

Rapamycin FKBP12

Rapamycin binds FKBP12.

Rapamycin doesn't work alone – it first has to team up with a helper protein called FKBP12.

Rapamycin is not an ordinary inhibitor: it first binds the small protein FKBP12, and only the two-part complex is the real drug.

The conditions it holds under

X-ray crystallography and in vitro work on bovine, rat and mouse material (CHO1996, BRO1994, SAB1995). Describes drug binding in purified systems; it says nothing about dose or effect in patients.

Time it takes
seconds
Step
direct (one molecule acts on the other)
Measured in
human cells
Where in the cell
cytosol
Reaches people?
plausible in people, not shown directly
How settled
settled in the literature

Studies behind it

YearEvidenceStudy
1996 M Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAPCHO1996 The crystal structure that showed HOW rapamycin works at the atomic level: one rapamycin molecule glues two proteins together - FKBP12 and mTOR's FRB domain - by plugging into two hydrophobic pockets at once. A textbook example of a small molecule acting as 'molecular glue' to force protein dimerization.
1994 M A mammalian protein targeted by G1-arresting rapamycin-receptor complexBRO1994 Purified FRAP (mTOR) as the mammalian FKBP12-rapamycin target homologous to yeast TOR1/2.
1995 M Isolation of a protein target of the FKBP12-rapamycin complex in mammalian cellsSAB1995 Isolated mTOR as the FKBP12-rapamycin-associated protein controlling G1-S progression.

Points the other way

No study in the Atlas contradicts this link. That means none in this curated set, not none in the literature.

Who has checked this

Checked by
No researcher outside the project has checked this link yet.
Curator sign-off
Not signed off yet. This link was drafted with AI help and has not been reviewed link by link; treat it as a proposal until it is.
Curated by
Oliver Barton, with AI help for drafting; see how links are checked.

“How settled” describes how far researchers in the field agree. It is not the same as the sign-off above, which only says whether a named curator has checked this page.

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