کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1180452 | 962855 | 2008 | 10 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: The extra C-terminal tail is involved in the conformation, stability changes and the N/C-domain interactions of the calmodulin-like protein from pearl oyster Pinctada fucata The extra C-terminal tail is involved in the conformation, stability changes and the N/C-domain interactions of the calmodulin-like protein from pearl oyster Pinctada fucata](/preview/png/1180452.png)
Pearl oyster Pinctada fucata calmodulin-like protein (PfCaLP), containing an extra tail (D150-K161) at the C-terminal, is a novel protein involved in the regulation of oyster calcium metabolism. The purpose of this study is to gain insight into the conformational characteristics of the N/C-domain of PfCaLP, especially the detailed contribution of the extra tail to the Ca2+/Mg2+-induced conformational changes, the stability of the intact PfCaLP molecule and its C-domain, as well as to the interdomain communications in PfCaLP. Our results demonstrate that a strong interaction exists between the hydrophilic tail and the C-domain of PfCaLP. The extra tail, through affecting the C-domain conformational changes, further influences the migration rate, conformational changes, N/C-domain interactions and exposure of the hydrophobic patches of the intact PfCaLP molecule. Furthermore, the tail could actively regulate the stability of PfCaLP and its C-domain. Our studies are helpful to explain our previous finding that the tail plays important roles in PfCaLP-target interaction in the oyster calcium metabolism.
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1784, Issue 11, November 2008, Pages 1514–1523