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cDNA cloning of a human 25 kDa FK506 and rapamycin binding protein.

作者信息

Hung D T, Schreiber S L

机构信息

Department of Chemistry, Harvard University, Cambridge, Massachusetts 02138.

出版信息

Biochem Biophys Res Commun. 1992 Apr 30;184(2):733-8. doi: 10.1016/0006-291x(92)90651-z.

Abstract

The abilities of FK506 and rapamycin to block distinct signal transduction pathways are mediated by soluble binding proteins. Previously, a family of these receptors has been recognized that includes a 25 kDa protein, FKBP25. We now report the isolation of a cDNA for FKBP25 from a human hippocampal cDNA library by oligonucleotide screening. The nucleotide sequence reveals an open reading frame that encodes a 224 amino acid polypeptide. Human FKBP25 shows 97% amino acid identity with bovine FKBP25 and 62% homology with human FKBP12.

摘要

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