TY - JOUR
T1 - Isolation of a human cDNA encoding a 25 kDa FK-506 and rapamycin binding protein
AU - Wiederrecht, Greg
AU - Martin, Mary M.
AU - Sigal, Nolan H.
AU - Siekierka, John J.
PY - 1992/5/29
Y1 - 1992/5/29
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0026717791&partnerID=8YFLogxK
U2 - 10.1016/S0006-291X(05)80990-8
DO - 10.1016/S0006-291X(05)80990-8
M3 - Article
C2 - 1376117
AN - SCOPUS:0026717791
SN - 0006-291X
VL - 185
SP - 298
EP - 303
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -