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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 Caenorhabditis elegans HER-1 and characterization of the interaction between HER-1 and TRA-2A.
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Crystal structure of Caenorhabditis elegans HER-1 and characterization of the interaction between HER-1 and TRA-2A.

机译：秀丽隐杆线虫HER-1的晶体结构和HER-1与TRA-2A相互作用的表征。

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摘要

HER-1 is a secreted protein that promotes male development in the nematode Caenorhabditis elegans. HER-1 inhibits the function of TRA-2A, a multipass integral membrane protein thought to serve as its receptor. We report here the 1.5-A crystal structure of HER-1. The structure was solved by the multiwavelength anomalous diffraction method by using selenomethionyl-substituted HER-1 produced in Chinese hamster ovary cells. The HER-1 structure consists of two all-helical domains and is not closely homologous to any known structure. Sites of amino acid substitutions known to impair HER-1 function were mapped on the HER-1 structure and classified according to the likely mechanism by which they affect HER-1 activity. A subset of these and other amino acid substitutions on the HER-1 surface were assayed for their ability to disrupt interactions between HER-1 and TRA-2A-expressing cells, and a localized region on the HER-1 surface important for mediating this interaction was identified.
机译：HER-1是一种分泌蛋白，可促进线虫秀丽隐杆线虫中的男性发育。 HER-1抑制TRA-2A的功能，TRA-2A是一种多通道整合膜蛋白，被认为是其受体。我们在这里报告HER-1的1.5-A晶体结构。通过使用中国仓鼠卵巢细胞中产生的硒代甲硫酰基取代的HER-1，通过多波长异常衍射法解析了该结构。 HER-1结构由两个全螺旋结构域组成，与任何已知结构都不紧密同源。将已知会破坏HER-1功能的氨基酸取代位点定位在HER-1结构上，并根据其影响HER-1活性的可能机制进行分类。测定了这些和其他氨基酸在HER-1表面上的子集破坏HER-1和TRA-2A表达细胞之间相互作用的能力，以及在HER-1表面上对于介导这种相互作用很重要的局部区域被确定。

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