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Intertwined structured and unstructured regions of exRAGE identified by monitoring hydrogen-deuterium exchange.

机译:通过监测氢-氘交换确定了exRAGE的缠绕结构和非结构区域。

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摘要

Receptor for advanced glycation end products (RAGE) is a multiligand receptor that is engaged in many pathological processes. Potentially beneficial modification of its activity requires sound knowledge of its structural properties. However, up to now, only the structures of its separated domains have been published or deposited in databases. In this work, we used hydrogen-deuterium exchange and mass spectrometry to gain insight into the structural properties of exRAGE (extracellular region of RAGE)--the full extracellular part of the protein. The present work indicates the common and disparate features of full exRAGE as compared to the structural models of its separate domains. The highlight of the present study is the contrasting behavior of the different regions of the protein, with the protected regions neighboring fully exposed parts especially in the N-terminal V domain.
机译:晚期糖基化终末产物(RAGE)的受体是一种多配体受体,参与许多病理过程。对其活性进行潜在的有益修饰需要对其结构性质有充分的了解。但是,到目前为止,只有其分离域的结构才被发布或存放在数据库中。在这项工作中,我们使用氢-氘交换和质谱法深入了解了exRAGE(RAGE的细胞外区域)的结构特性-exRAGE是蛋白质的完整细胞外部分。目前的工作表明完全exRAGE与其共同域的结构模型相比的共同特征和不同特征。本研究的重点是蛋白质不同区域的对比行为,其中受保护区域邻近完全暴露的部分,尤其是在N末端V结构域。

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