IR@PKUHSC  > 北京大学药学院  > 化学生物学系
学科主题药学
Binding of La3+ to calmodulin and its effects on the interaction between calmodulin and calmodulin binding peptide, polistes mastoparan
Hu, J; Jia, X; Li, Q; Yang, XD; Wang, K
刊名BIOCHEMISTRY
2004-03-16
DOI10.1021/bi035784i
43期:10页:2688-2698
收录类别SCI
文章类型Article
WOS标题词Science & Technology
类目[WOS]Biochemistry & Molecular Biology
研究领域[WOS]Biochemistry & Molecular Biology
关键词[WOS]CALCIUM-FREE CALMODULIN ; NITRIC-OXIDE SYNTHASE ; HIGH-AFFINITY BINDING ; LIGHT-CHAIN KINASE ; EUROPIUM(III) LUMINESCENCE ; LANTHANIDE IONS ; CELLS ; CA-2 ; DISSOCIATION ; KINETICS
英文摘要

Binding of La3+ to calmodulin (CaM) and its effects on the complexes of CaM and CaM-binding peptide, polistes mastoparan (Mas), were investigated by nuclear magnetic resonance (NMR) spectroscopy, fluorescence and circular dichroism spectroscopy, and by the fluorescence stopped-flow method. The four binding sites of La3+ on CaM were identified as the same as the binding sites of Ca2+ on CaM through NMR titration of La3+ to uniformly N-15-labeled CaM. La3+ showed a slightly higher affinity to the binding sites on the N-terminal domain of CaM than that to the C-terminal. Large differences between the H-1-N-15 heteronuclear single quantum coherence (HSQC) spectra of Ca4CaM and La4CaM suggest conformational differences between the two complexes. Fluorescence and CD spectra also exhibited structural differences. In the presence of Ca2+ and La3+, a hybrid complex, Ca2La2CaM, was formed, and the binding of La3+ to the N-terminal domain of CaM seemed preferable over binding to the C-terminal domain. Through fluorescence titration, it was shown that La4CaM and Ca2La2CaM had similar affinities to Mas as Ca4CaM. Fluorescence stopped-flow experiments showed that the dissociation rate of La3+ from the C-terminal domain of CaM was higher than that from the N-terminal. However, in the presence of Mas, the dissociation rate of La3+ decreased and the dissociation processes from both global domains were indistinguishable. In addition, compared with the case of Ca4CaM-Mas, the slower dissociations of Mas from La4CaM-Mas and Ca2La2CaM-Mas complexes indicate that in the presence of La3+, the CaM-Mas complex became kinetically inert. A possible role of La3+ in the Ca2+-CaM-dependent pathway is discussed.

语种英语
WOS记录号WOS:000220143300003
Citation statistics
Cited Times:28[WOS]   [WOS Record]     [Related Records in WOS]
文献类型期刊论文
条目标识符http://ir.bjmu.edu.cn/handle/400002259/55154
Collection北京大学药学院_化学生物学系
作者单位1.Peking Univ, Natl Res Labs Nat & Biomimet Drugs, Beijing 100083, Peoples R China
2.Peking Univ, Sch Pharmaceut Sci, Dept Biol Chem, Beijing 100083, Peoples R China
Recommended Citation
GB/T 7714
Hu, J,Jia, X,Li, Q,et al. Binding of La3+ to calmodulin and its effects on the interaction between calmodulin and calmodulin binding peptide, polistes mastoparan[J]. BIOCHEMISTRY,2004,43(10):2688-2698.
APA Hu, J,Jia, X,Li, Q,Yang, XD,&Wang, K.(2004).Binding of La3+ to calmodulin and its effects on the interaction between calmodulin and calmodulin binding peptide, polistes mastoparan.BIOCHEMISTRY,43(10),2688-2698.
MLA Hu, J,et al."Binding of La3+ to calmodulin and its effects on the interaction between calmodulin and calmodulin binding peptide, polistes mastoparan".BIOCHEMISTRY 43.10(2004):2688-2698.
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