Wiederrecht G, Martin M M, Sigal N H, Siekierka J J
Department of Immunology Research, Merck Research Labs, Rahway, New Jersey 07065.
Biochem Biophys Res Commun. 1992 May 29;185(1):298-303. doi: 10.1016/s0006-291x(05)80990-8.
Recently, the nearly complete peptide sequence of a 25 kDa rapamycin and FK-506 binding protein that had been isolated from calf thymus, brain, and spleen was reported (1). Based upon the amino acid sequence of this bovine protein, bFKBP25, we have isolated from a JURKAT cDNA library the cDNA encoding the human homolog, hFKBP25. Translation of the open reading frame contained within this cDNA clone yields a sequence that, in its C-terminal half, is 41% identical to the major human FK-506 binding protein, hFKBP12, and 43% identical to hFKBP13. The N-terminal half of hFKBP25 is unrelated to any known protein.
