Structure of the transmembrane signal initiation site of the relaxin-like factor (RLF/INSL3).
Structure of the transmembrane signal initiation site of the relaxin-like factor (RLF/INSL3).
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松弛素样因子 (RLF/INSL3) 跨膜信号起始位点的结构。
DOI：
10.1021/bi700708s
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发表时间：
2007
期刊：
影响因子：
2.9
通讯作者：
Schwabe,Christian
中科院分区：
文献类型：
--
作者：
Bullesbach,ErikaE;Schwabe,Christian
我们发现了松弛素样因子的信号起始结构，并表明其功能独立于接触区的氨基酸侧链。本文提供的证据表明，信号诱导是肽键的功能，并且信号接触的完成是通过配体与富含亮氨酸的重复 G 蛋白偶联受体 8 (LGR8) 的结合启动的。特定的结合模式迫使某些肽键进入信号位置。这一观察结果意味着接收结构同样是非特异性的，因此信号传导应该发生在受体的任何肽键或受体结合配体的信号线范围内的跨膜环处。我们的观察结果为配体串扰以及某些抗体引发通常与特定配体相关的生物反应的能力提供了解释。
We have discovered the signal initiation structure of the relaxin-like factor and shown its function to be independent of the amino acid side chains in the contact region. Evidence presented in this article suggests that signal induction is a function of the peptide bond and that completion of the signaling contact is initiated by ligand binding to the leucine-rich repeat G-protein coupled receptor 8 (LGR8). The specific mode of binding forces certain peptide bonds into a signaling position. This observation implies that the receiving structures are equally nonspecific so that signaling should occur at any peptide bond of the receptor or the trans-membrane loop that is within reach of the signaling wires of the receptor-bound ligand. Our observations offer an explanation for ligand cross-talk as well as for the ability of some antibodies to elicit the biological response normally associated with a specific ligand.