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Peptidyl-prolyl cis-trans isomerase FKBP11 (FKBP11) is a member of the FKBP family of enzymes that catalyze the cis-trans isomerization of proline residues in polypeptide chains, a critical process in protein folding[2][6]. Unlike related family members, FKBP11 is a transmembrane protein localized in the endoplasmic reticulum (ER), where it functions as a translocon accessory factor, aiding the synthesis and biogenesis of secretory and membrane proteins with long ER-lumenal segments[1]. FKBP11 is most highly expressed in specialized secretory cells and is transcriptionally upregulated under conditions of ER stress[1]. It is implicated in bone formation, immune cell function (notably B-cell tolerance and plasma cell differentiation), and may play a role in diseases linked to defective protein folding and the secretory pathway[1][2]. Its enzymatic activity is inhibited by the immunosuppressant drugs FK506 (tacrolimus) and rapamycin (sirolimus)[2][6].
Immunosuppressants (FK506, rapamycin) inhibit FKBP11's peptidyl-prolyl isomerase activity by direct binding[2][6]
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