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首页> 外文期刊>Journal of Leukocyte Biology: An Official Publication of the Reticuloendothelial Society >New insights into the structure and function of chemokine receptor:chemokine complexes from an experimental perspective
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New insights into the structure and function of chemokine receptor:chemokine complexes from an experimental perspective

机译:趋化因子受体的结构和功能的新见解:实验视角下的趋化因素

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Abstract Chemokines are small soluble proteins that drive cell migration through the formation of concentration gradients. Chemokine binding to G protein‐coupled chemokine receptors in the cell membrane activates intracellular signaling pathways and is a fundamental process involved in numerous physiological and pathophysiological functions. In the past few years, significant experimental developments have made it possible to characterize complexes between chemokine receptors and chemokines at a molecular level. Here, I review these developments from an experimental perspective, focusing on how the ability to express, purify, and stabilize receptor:chemokine complexes have made studies by X‐ray crystallography, nuclear magnetic resonance, and other methods possible. I give examples of how these studies have advanced our understanding of the architecture of receptor:chemokine complexes as well as the mechanisms involved in complex formation. Finally, I discuss some of the many remaining questions and challenges that will require studies of more receptors and chemokines as well as further development of experimental methods.
机译:摘要趋化因子是通过形成浓度梯度来驱动细胞迁移的小可溶性蛋白质。趋化因子结合到细胞膜中的G蛋白偶联趋化因子受体激活细胞内信号通路,并且是涉及许多生理和病理生理功能的基本过程。在过去几年中,显着的实验性能使得在分子水平下表征趋化因子受体和趋化因子之间的复合物。在这里,我从实验的角度审查了这些发展,重点是如何表达,净化和稳定受体的能力:趋化因子已经通过X射线晶体学,核磁共振和其他方法进行了研究。我举例说明这些研究如何先进我们对受体结构的理解:趋化因素以及参与复杂形成的机制。最后,我讨论了一些剩下的一些问题和挑战,需要研究更多的受体和趋化因子以及实验方法的进一步发展。

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