کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10869912 | 1073978 | 2015 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The closed conformation of the LDL receptor is destabilized by the low Ca++ concentration but favored by the high Mg++ concentration in the endosome
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The LDL receptor (LDLR) internalizes LDL and VLDL particles. In the endosomes, it adopts a closed conformation important for recycling, by interaction of two modules of the ligand binding domain (LR4-5) and a β-propeller motif. Here, we investigate by SPR the interactions between those two modules and the β-propeller. Our results indicate that the two modules cooperate to bind the β-propeller. The binding is favored by low pH and by high [Ca++]. Our data show that Mg++, at high concentration in the endosome, favors the formation of the closed conformation by replacing the structuring effect of Ca++ in LR5. We propose a sequential model of LDL release where formation of the close conformation follows LDL release.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 589, Issue 23, 30 November 2015, Pages 3534-3540
Journal: FEBS Letters - Volume 589, Issue 23, 30 November 2015, Pages 3534-3540
نویسندگان
Juan MartÃnez-Oliván, Xabier Arias-Moreno, Ramón Hurtado-Guerrero, José Alberto Carrodeguas, Laura Miguel-Romero, Alberto Marina, Pierpaolo Bruscolini, Javier Sancho,