ESR Study on calcineurin
X-band electron spin resonance spectroscopy was used to investigate the binding of Mn2+tothe apo-forms of calcineurin and its A and B subunits.The results indicated the presence of 2Mn2+binding sites of different affinities(20μmol/L and 60μmol/L)in the calcineurin A subunit and 4Mn2+binding sites in...
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Veröffentlicht in: | 中国科学:化学英文版 1995 (9), p.1117-1122 |
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description | X-band electron spin resonance spectroscopy was used to investigate the binding of Mn2+tothe apo-forms of calcineurin and its A and B subunits.The results indicated the presence of 2Mn2+binding sites of different affinities(20μmol/L and 60μmol/L)in the calcineurin A subunit and 4Mn2+binding sites in the calcineurin subunit B,2 high affinity and 2 low affinity binding sites withKd’s of 4μmol/L and 90μmol/L,respectively.Interestingly and quite surprisingly,Mn2+binding to theholoenzyme was characterized by only 2 binding sites with Kd’s of 7μmol/L and 33μmol/L.However,inthe presence of calmodulin about 10 Mn2+sites were detected,and the Mn2+calmodulin-calcineurin complexexhibited enzymatic activity.These results,based on direct spectral measurements of the metal ligand,demonstrate that Mn2+binds to both free subunits of calcineurin in a manner distinct from binding to theholoenzyme.Also,the data suggest that conformational changes occur upon heterodimer formation andassociation of the holoenzyme with the regulatory protein calmodulin. |
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subjects | calcineurin calmodulin ESR |
title | ESR Study on calcineurin |
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