title: Interaction of glycyrol with calcineurin A studied by spectroscopic methods and docking.
abstract: We have shown previously that glycyrol has an inhibitory effect on the immune response in mice by reducing calcineurin activity (Li et al., 2010, Pharm Biol 48:1177–1184). Here, we investigated the interaction of glycyrol with calcineurin A (CNA, catalytic A subunit of calcineurin) by spectroscopic methods and docking. We showed that glycyrol binds to CNA via hydrophobic interactions in a ratio of 1:1, and the main binding site is in the catalytic domain of CNA close to the calcineurin B subunit-binding domain. Binding of glycyrol changes the secondary structure of CNA, and this effect may possibly inhibit CN activity.
authors.affiliation: Department of Biochemistry and Molecular Biology, Beijing Normal University, Beijing, China.
authors.forename: Liqin
authors.initials: L
authors.lastname: Peng
authors.forename: Yao
authors.initials: Y
authors.lastname: Qi
authors.forename: Hezhen
authors.initials: H
authors.lastname: Wu
authors.forename: Qun
authors.initials: Q
authors.lastname: Wei
mesh_terms: D019703:Calcineurin / Q000737:chemistry* / Q000235:genetics; D002942:Circular Dichroism; D004735:Energy Transfer; D005990:Glycerol / Q000737:chemistry*; D008958:Models, Molecular; D009154:Mutation; D017433:Protein Structure, Secondary; D013057:Spectrum Analysis / Q000379:methods*
chemical_list: D019703:Calcineurin; D005990:Glycerol