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PubMed · 1371698

A rapamycin-selective 25-kDa immunophilin.

A Galat·W S Lane·R F Standaert·S L Schreiber
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Abstract

FKBP25, a previously uncharacterized 25-kDa FK506- and rapamycin-binding protein, was purified to homogeneity from calf thymus, brain, and spleen, and the sequence of a 215 amino acid (aa) 24-kDa C-terminal peptide was established. The N-terminal domain (101 aa) is unrelated to any known protein, is hydrophilic, and is predicted by circular dichroism spectroscopy to be largely alpha-helix. The C-terminal domain (114 aa) is homologous to FKBP12 and other FKBPs but has a potential nuclear targeting sequence and a unique insertion of seven amino acids in one of its loops. FKBP25 displays the rotamase activity characteristic of FKBPs; the activity is inhibited by the immunosuppressants rapamycin (Ki = 0.9 nM) and FK506 (Ki = 160 nM), but not cyclosporin A. The protein, its rapamycin selectivity, and the potential nuclear targeting sequence are discussed in terms of the structure of hFKBP12.

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Amino Acid SequenceAnimalsAntifungal AgentsBrainCarrier ProteinsCattleCircular DichroismCyclohexanolsDatabases, FactualImmunosuppressive AgentsMolecular Sequence DataMolecular WeightPeptidesPolyenesProtein ConformationPyransSequence AlignmentSirolimusSpleenTacrolimusThymus GlandJournal ArticleResearch Support, U.S. Gov't, P.H.S.

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A Galat, W S Lane, R F Standaert, S L Schreiber. 1992-03-03. A rapamycin-selective 25-kDa immunophilin.. https://doi.org/10.1021/bi00123a031

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