The closed conformation of the LDL receptor is destabilized by the low Ca++ concentration but favored by the high Mg++ concentration in the endosome
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- 作者：Juan Martí ; nez-Olivá ; na ; b ; c ; Xabier Arias-Morenoa ; b ; Ramó ; n Hurtado-Guerreroa ; c ; d ; José ; Alberto Carrodeguasa ; b ; c ; Laura Miguel-Romeroe ; Alberto Marinae ; Pierpaolo Bruscolinia ; Javier Sanchoa ; b ; c ; jsancho@unizar.es" class="auth_mail" title="E-mail the corresponding author
- 关键词：Low density lipoprotein receptor ; Surface plasmon resonance ; Binding ; Endosome
- 刊名：FEBS Letters
- 出版年：2015
- 出版时间：30 November 2015
- 年：2015
- 卷：589
- 期：23
- 页码：3534-3540
- 全文大小：1062 K
文摘
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The interactions between L4/L5 repeats in LDLR and the β-propeller are determined.
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The two modules cooperate to bind the β-propeller.
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The binding is favored by low pH and by high [Ca++].
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Mg++ favors the formation of the closed conformation.
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We propose that the formation of the closed conformation follows LDL release.