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Isolation of a cDNA encoding a novel human FK506-binding protein homolog containing leucine zipper and tetratricopeptide repeat motifs.

作者信息

Lam E, Martin M, Wiederrecht G

机构信息

Department of Immunology Research, Merck Research Laboratories, Rahway, NJ 07065, USA.

出版信息

Gene. 1995 Jul 28;160(2):297-302. doi: 10.1016/0378-1119(95)00216-s.

DOI:10.1016/0378-1119(95)00216-s
PMID:7543869
Abstract

Reduced-stringency PCR was used to isolate a cDNA encoding a novel human FK506-binding protein (FKBP) homolog. The encoded 38-kDa protein (FKBPr38) contains at its N-terminus a domain that is 33% identical to FKBP12. FKBPr38 is a member of a subclass of immunophilins, whose other members include FKBP52 and CyP40 (cyclophilin 40), that contain a three-unit tetratricopeptide repeat (TPR). In addition, FKBPr38 contains a consensus leucine-zipper repeat. The presence of the TPR domain and leucine zipper suggest that FKBPr38 may form homo-multimers or interact with other, as yet unidentified, proteins.

摘要

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