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

Biochem Biophys Res Commun

Authors	D Hung S Schreiber
Keywords	Animals Humans Base Sequence Molecular Sequence Data Amino Acid Sequence Carrier Proteins Open Reading Frames Cloning, Molecular Gene Library Oligodeoxyribonucleotides Sequence Homology, Nucleic Acid Cattle Molecular Weight Polyenes Sirolimus Tacrolimus Immunosuppressive Agents Tacrolimus Binding Proteins Oligonucleotide Probes
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.
Year of Publication	1992
Journal	Biochem Biophys Res Commun
Volume	184
Issue	2
Pages	733-8
Date Published	1992 Apr 30
ISSN	0006-291X
PubMed ID	1374240
Links	PubMed Google Scholar
Grant list	T32 GM007753 / GM / NIGMS NIH HHS / United States 2-T32-GM07753-11 / GM / NIGMS NIH HHS / United States GM-38627 / GM / NIGMS NIH HHS / United States

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