Human T cell cyclophilin18 binds to thiol-specific antioxidant protein Aop1 and stimulates its activity

Autor:	A, Jäschke, H, Mi, M, Tropschug
Rok vydání:	1998
Předmět:	Peroxiredoxin III Base Sequence Recombinant Fusion Proteins T-Lymphocytes Peroxiredoxins Saccharomyces cerevisiae In Vitro Techniques Peptidylprolyl Isomerase Antioxidants Neoplasm Proteins Oxidative Stress Peroxidases Humans Sulfhydryl Compounds DNA Primers Protein Binding
Zdroj:	Journal of molecular biology. 277(4)
ISSN:	0022-2836
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=pmid________::9566abdfb98e7d420028c6522bb2e8c3 https://pubmed.ncbi.nlm.nih.gov/9545370 Zobrazit plný text záznamu Full Text from ScienceDirect