Human cyclophilin B: a second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequence.
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منابع مشابه
Human cyclophilin B: a second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequence.
We report the cloning and characterization of a cDNA encoding a second human cyclosporin A-binding protein (hCyPB). Homology analyses reveal that hCyPB is a member of the cyclophilin B (CyPB) family, which includes yeast CyPB, Drosophila nina A, and rat cyclophilin-like protein. This family is distinguished from the cyclophilin A (CyPA) family by the presence of endoplasmic reticulum (ER)-direc...
متن کاملPreliminary characterization of a cloned neutral isoelectric form of the human peptidyl prolyl isomerase cyclophilin.
We report the cloning of a neutral isoelectric form of the human peptidyl prolyl isomerase, cyclophilin, its expression in Escherichia coli, and its purification and comparison to bovine thymus cyclophilin. The cloned protein exhibited a pI of approximately 7.8 and formed a simple 1:1 complex with cyclosporin A. This cloned form had a pI similar to that observed for the neutral isoform (pI appr...
متن کاملRegulation of the tyrosine kinase Itk by the peptidyl-prolyl isomerase cyclophilin A.
Interleukin-2 tyrosine kinase (Itk) is a nonreceptor protein tyrosine kinase of the Tec family that participates in the intracellular signaling events leading to T cell activation. Tec family members contain the conserved SH3, SH2, and catalytic domains common to many kinase families, but they are distinguished by unique sequences outside of this region. The mechanism by which Itk and related T...
متن کاملThe gene for cyclophilin (peptidyl-prolyl cis-trans isomerase) from Schizosaccharomyces pombe.
Cyclophilin (CPH) is an ubiquitous 17-kD cytosolic protein with high binding affinity for the immunosuppressant cyclosporin A (1). CPH is identical to peptidyl-prolyl cis-trans isomerase, an enzyme catalyzing the isomerisation of proline imidic peptide bonds in oligopeptides and accelerating the rate-limiting steps in the refolding of certain proteins in vitro (2, 3). We have used degenerate an...
متن کاملThe characterization of a cyclophilin-type peptidyl prolyl cis-trans-isomerase from the endoplasmic-reticulum lumen.
A luminally located peptidyl prolyl cis-trans-isomerase (PPI) has been purified from bovine liver microsomes. It has a molecular mass of 20.6 kDa, and N-terminal sequencing demonstrates strong sequence similarity to the sequences of the cyclophilin B family. The enzyme catalyses the isomerization of the standard proline-containing peptide N-succinyl-Ala-Ala-Pro-Phe p-nitroanilide, as well as th...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1991
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.88.5.1903