• 主题
高级搜索  >
历史搜索 清空历史
首页> 美国卫生研究院文献>Acta Crystallographica Section D: Biological Crystallography >Structural insights into the binding of the human receptor for advanced glycation end products (RAGE) by S100B as revealed by an S100B–RAGE-derived peptide complex
【2h】

Structural insights into the binding of the human receptor for advanced glycation end products (RAGE) by S100B as revealed by an S100B–RAGE-derived peptide complex

机译：S100B–RAGE衍生的肽复合物揭示了对S100B对人类受体与高级糖基化终产物（RAGE）的结合的结构见解

代理获取
本网站仅为用户提供外文OA文献查询和代理获取服务，本网站没有原文。下单后我们将采用程序或人工为您竭诚获取高质量的原文，但由于OA文献来源多样且变更频繁，仍可能出现获取不到、文献不完整或与标题不符等情况，如果获取不到我们将提供退款服务。请知悉。
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

S100B is a damage-associated molecular pattern protein that, when released into the extracellular milieu, triggers initiation of the inflammatory response through the receptor for advanced glycation end products (RAGE). Recognition of S100B is accomplished via the amino-terminal variable immunoglobulin domain (V-domain) of RAGE. To gain insights into this interaction, a complex between S100B and a 15-amino-acid peptide derived from residues 54–68 of the V-domain was crystallized. The X-ray crystal structure was solved to 2.55 Å resolution. There are two dimers of S100B and one peptide in the asymmetric unit. The binding interface of this peptide is compared with that found in the complex between S100B and the 12-amino-acid CapZ-derived peptide TRTK-12. This comparison reveals that although the peptides adopt completely different backbone structures, the residues buried at the interface interact with S100B in similar regions to form stable complexes. The binding affinities of S100B for the intact wild-type V-domain and a W61A V-domain mutant were determined to be 2.7 ± 0.5 and 1.3 ± 0.7 µM, respectively, using fluorescence titration experiments. These observations lead to a model whereby conformational flexibility in the RAGE receptor allows the adoption of a binding conformation for interaction with the stable hydrophobic groove on the surface of S100B.
机译：S100B是一种与损伤相关的分子模式蛋白，当释放到细胞外环境中时，会通过高级糖基化终产物（RAGE）的受体触发炎症反应的启动。 S100B的识别是通过RAGE的氨基末端可变免疫球蛋白结构域（V域）实现的。为了深入了解这种相互作用，结晶了S100B和源自V域第54-68位残基的15个氨基酸的肽之间的复合物。 X射线晶体结构解析为2.55Å分辨率。不对称单元中有两个S100B二聚体和一个肽。将该肽的结合界面与在S100B和CapZ衍生的12个氨基酸的肽TRTK-12之间的复合物中发现的结合界面进行了比较。该比较表明，尽管肽采用完全不同的骨架结构，但掩埋在界面上的残基在相似区域与S100B相互作用形成稳定的复合物。使用荧光滴定实验确定，S100B与完整野生型V结构域和W61A V结构域突变体的结合亲和力分别为2.7±0.5和1.3±0.7μm。这些观察结果导致了一个模型，在该模型中，RAGE受体的构象柔韧性允许采用结合构象，以与S100B表面的稳定疏水沟相互作用。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
代理获取

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号