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Article

Rapamycin analogs with differential binding specificity permit orthogonal control of protein activity.

Chemistry & biology - 1 Jan 2006

Bayle J Henri, Grimley Joshua S, Stankunas Kryn, Gestwicki Jason E, Wandless Thomas J, Crabtree Gerald R

Abstract excerpt

Controlling protein dimerization with small molecules has broad application to the study of protein function. Rapamycin has two binding surfaces: one that binds to FKBP12 and the other to the Frb domain of mTor/FRAP, directing their dimerization. Rapamycin is a potent cell growth inhibitor, but chemical modification of the surface contacting Frb alleviates this effect. Productive interactions with Frb-fused...

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Identifiers

PMID: 16426976
DOI: 10.1016/j.chembiol.2005.10.017

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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