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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Crystal structure of human junctional adhesion molecule 1: implications for reovirus binding.
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Crystal structure of human junctional adhesion molecule 1: implications for reovirus binding.

机译：人连接黏附分子的晶体结构1：呼肠孤病毒结合的含义。

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摘要

Reovirus attachment to cells is mediated by the binding of viral attachment protein sigma 1 to junctional adhesion molecule 1 (JAM1). The crystal structure of the extracellular region of human JAM1 (hJAM1) reveals two concatenated Ig-type domains with a pronounced bend at the domain interface. Two hJAM1 molecules form a dimer that is stabilized by extensive ionic and hydrophobic contacts between the N-terminal domains. This dimeric arrangement is similar to that observed previously in the murine homolog of JAM1, indicating physiologic relevance. However, differences in the dimeric structures of hJAM1 and murine JAM1 suggest that the interface is dynamic, perhaps as a result of its ionic nature. We demonstrate that hJAM1, but not the related proteins hJAM2 and hJAM3, serves as a reovirus receptor, which provides insight into sites in hJAM1 that likely interact with sigma 1. In addition, we present evidence that the previously reported structural homology between sigma 1 and the adenovirus attachment protein, fiber, also extends to their respective receptors, which form similar dimeric structures. Because both receptors are located at regions of cell-cell contact, this similarity suggests that reovirus and adenovirus use conserved mechanisms of entry and pathways of infection.
机译：呼肠孤病毒与细胞的附着是通过病毒附着蛋白sigma 1与结合黏附分子1（JAM1）的结合而介导的。人JAM1（hJAM1）胞外区的晶体结构揭示了两个串联的Ig型结构域，在结构域界面处有明显的弯曲。两个hJAM1分子形成一个二聚体，该二聚体通过N端结构域之间的广泛离子和疏水接触得以稳定。该二聚体排列类似于先前在JAM1的鼠同源物中观察到的排列，表明生理相关性。但是，hJAM1和鼠类JAM1的二聚体结构差异表明该界面是动态的，这可能是由于其离子性质所致。我们证明hJAM1，而不是相关蛋白hJAM2和hJAM3，充当呼肠孤病毒受体，可提供对hJAM1中可能与sigma 1相互作用的位点的洞察力。此外，我们还提供了先前报道的sigma 1和sigma之间结构同源的证据腺病毒附着蛋白纤维也延伸到它们各自的受体，形成相似的二聚体结构。因为这两个受体都位于细胞与细胞接触的区域，所以这种相似性表明呼肠孤病毒和腺病毒使用保守的进入机制和感染途径。

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