Abstract：
:Quercetin, the primary dietary flavonol, exerts a strong inhibitory effect on calcineurin (CN), a unique Ca(2+)/calmodulin-dependent serine/threonine protein phosphatase. Using fluorescence spectroscopy (FS) we showed quercetin strongly bound to calcineurin catalytic subunit (CNA) with a ratio of 1:1; we also showed that calcineurin regulatory subunit (CNB) weakened this binding. In addition, the secondary structure of CNA was much tighter in the presence of quercetin. An FS study with CNA truncated mutant CNAa showed that the binding area for quercetin was reduced to the catalytic domain of CNA. Furthermore, fluorescence resonance energy transfer (FRET) results and molecular docking indicated three potential binding sites for quercetin, which were located at a region between the active centre of CNA and the CNB binding domain, a similar binding area to that of cyclosporin A and tacrolimus. Interestingly, this region was also important for CN substrate recognition.
journal_name
Food Chemjournal_title
Food chemistryauthors
Lei H,Luo J,Tong L,Peng LQ,Qi Y,Jia ZG,Wei Qdoi
10.1016/j.foodchem.2011.01.119subject
Has Abstractpub_date
2011-08-01 00:00:00pages
1169-74issue
3eissn
0308-8146issn
1873-7072pii
S0308-8146(11)00226-3journal_volume
127pub_type
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