Studies on the interactions of kaempferol to calcineurin by spectroscopic methods and docking.
Biochim Biophys Acta
; 1794(8): 1269-75, 2009 Aug.
Article
en En
| MEDLINE
| ID: mdl-19439201
ABSTRACT
Kaempferol, in our previous study, was a new immunosuppressant on calcineurin (CN), the Ca(2+)/calmodulin (CaM)-dependent protein phosphatase. Here, we examined the interactions of kaempferol with CN by fluorescence spectroscopy (FS), circular dichroism spectroscopy (CD) and docking. Data of kaempferol with CN catalytic subunit (CN A) and its truncated mutant CNAa obtained by FS method showed that the binding stoichiometry of kaempferol/CN A was 11, catalytic domain of CN A was the concrete domain for kaempferol binding while other domains contributed a lot to this binding. Distances from kaempferol to each tryptophan (Trp) in CN A by energy transfer experiments and the subsequent docking study interestingly provided the same binding sites for kaempferol, which all located in the non-active site area of CN A catalytic domain, also consisted with our previous conclusion from CN activity assay. Furthermore, CD results showed a much tighter structure of CN A for the inhibitor binding; on the other hand, presence of Ca(2+) and Mn(2+) decreased kaempferol binding on CN A.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Calcineurina
/
Quempferoles
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Biochim Biophys Acta
Año:
2009
Tipo del documento:
Article
País de afiliación:
China