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首页> 外文期刊>Acta crystallographica. Section D, Biological crystallography. >Interaction of the amyloid precursor protein-like protein 1 (APLP1) E2 domain with heparan sulfate involves two distinct binding modes
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Interaction of the amyloid precursor protein-like protein 1 (APLP1) E2 domain with heparan sulfate involves two distinct binding modes

机译：淀粉样前体蛋白质像的交互与硫酸乙酰肝素蛋白1 (APLP1) E2域涉及到两个不同的绑定模式

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摘要

Beyond the pathology of Alzheimer's disease, the members of the amyloid precursor protein (APP) family are essential for neuronal development and cell homeostasis in mammals. APP and its paralogues APP-like protein 1 (APLP1) and APP-like protein 2 (APLP2) contain the highly conserved heparan sulfate (HS) binding domain E2, which effects various (patho)physiological functions. Here, two crystal structures of the E2 domain of APLP1 are presented in the apo form and in complex with a heparin dodecasaccharide at 2.5 angstrom resolution. The apo structure of APLP1 E2 revealed an unfolded and hence flexible N-terminal helix alpha A. The (APLP1 E2) 2-(heparin) 2 complex structure revealed two distinct binding modes, with APLP1 E2 explicitly recognizing the heparin terminus but also interacting with a continuous heparin chain. The latter only requires a certain register of the sugar moieties that fits to a positively charged surface patch and contributes to the general heparin-binding capability of APP-family proteins. Terminal binding of APLP1 E2 to heparin specifically involves a structure of the nonreducing end that is very similar to heparanase-processed HS chains. These data reveal a conserved mechanism for the binding of APP-family proteins to HS and imply a specific regulatory role of HS modifications in the biology of APP and APP-like proteins.
机译：除了阿尔茨海默病的病理淀粉样前体蛋白(APP)的成员家庭对于神经发展,至关重要在哺乳动物细胞内稳态。paralogues中蛋白1 (APLP1)和中蛋白2 (APLP2)包含高度守恒的硫酸乙酰肝素(HS)绑定域E2,影响各种(patho)生理功能。域的APLP1 apo形式和介绍在复杂的肝素dodecasaccharide为2.5埃分辨率。E2透露一个展开,因此灵活氨基端螺旋阿尔法a (APLP1 E2)(2) -肝素2复杂结构揭示了两个不同的绑定模式,明确APLP1 E2认识到肝素终点站也与连续交互肝素链。后者只需要一定的登记适合糖根带正电表面贴片和有助于一般heparin-binding APP-family能力蛋白质。具体涉及到的结构nonreducing结束非常相似heparanase-processed HS链。保守的绑定机制APP-family HS和暗示特定的蛋白质修改商品的监管作用生物学的应用和中蛋白质。

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