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FK-506 binding protein from Tolypocladium inflatum: resistance of FKBP/FK-506 complex against proteolysis.

作者信息

Lee C, Hoffmann K, Zocher R

机构信息

Institut für Biochemie und Molekulare Biologie, Technische Universität Berlin, FRG.

出版信息

Biochem Biophys Res Commun. 1992 Feb 14;182(3):1282-7. doi: 10.1016/0006-291x(92)91871-m.

Abstract

A 12-kDa peptidyl-prolyl-cis/trans-isomerase was purified 225-fold to homogeneity from the cyclosporin producing fungus Tolypocladium inflatum. The enzyme is highly sensitive to the immunosuppressant FK-506 but not to cyclosporin and thus belongs to the class of FK-506 binding proteins (FKBP). Interestingly the FKBP/FK-506 complex is resistant against proteolytic digestion by the endoproteases GluC and LysC, in contrast to the free FKBP, which is readily cleaved by these proteases. This protection may play a role in the effects of FK-506 in the living cell.

摘要

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