Human T cell cyclophilin18 binds to thiol-specific antioxidant protein Aop1 and stimulates its activity 1 1Edited by M. Yaniv

Autor:	Maximilian Tropschug, Anja Jäschke, Huaifeng Mi
Rok vydání:	1998
Předmět:	chemistry.chemical_classification T cell Isomerase Biology Protein–protein interaction Cytosol medicine.anatomical_structure Enzyme Biochemistry chemistry Structural Biology Cyclosporin a medicine Peroxiredoxin Molecular Biology Cyclophilin
Zdroj:	Journal of Molecular Biology. 277:763-769
ISSN:	0022-2836
DOI:	10.1006/jmbi.1998.1644
Popis:	Cyclophilins (CyPs) define a family of proteins binding to the immunosuppressive drug cyclosporin A (CsA). They are evolutionary highly conserved proteins being present in both pro- and eukaryotes and in different subcellular locations. CyPs possess enzymatic activity, namely peptidyl-prolyl cis-trans isomerase (PPIase) activity and are involved in cellular protein folding and protein interactions. Here we describe a novel interaction of human T cell cyclophilin18 (hCyP18). Abundant cytosolic hCyP18 binds to the thiol-specific antioxidant protein Aop1 and stimulates its enzymatic activity. Aop1 belongs to a family of proteins thought to be involved in defense of oxidative stress. The interaction of both proteins seem to be specific, since other PPIases do not have any stimulatory effect on Aop1.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::f4cc0cb00e15988f235979a1a0d19abe https://doi.org/10.1006/jmbi.1998.1644 Zobrazit plný text záznamu Full Text from ScienceDirect