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. 2018 Dec 5;9:1425. doi: 10.3389/fphar.2018.01425

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Copyright © 2018 Kolos, Voll, Bauder and Hausch.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Structures of FKBPs and their interaction partners. (A) Structure of FKBP51 (pdb-ID: 1KT0). The FK1 domain is depicted in red, the FK2 domain in green, TPR domains in blue. The pale-yellow region corresponds to a putative calmodulin binding domain. (B) Superposition of the FK506-binding domains of FKBP12 (1FKJ, green), FKBP13 (4NNR, gray), FKBP25 (5D75, blue), FKB51 (3O5R, yellow), and FKBP52 (4LAX, salmon). The conserved active site residues are highlighted as sticks, the bound FK506 is omitted for clarity. (C) Inhibitory complex (1TC0) of FKBP12 (green), FK506 (pink sticks), and calcineurin (cyan and blue).