...
首页> 外文期刊>Molecular cell >The structure of SOCS3 reveals the basis of the extended SH2 domain function and identifies an unstructured insertion that regulates stability
【24h】

The structure of SOCS3 reveals the basis of the extended SH2 domain function and identifies an unstructured insertion that regulates stability

机译:SOCS3的结构揭示了扩展的SH2域功能的基础,并确定了调节稳定性的非结构化插入

获取原文
获取原文并翻译 | 示例
   

获取外文期刊封面封底 >>

       

摘要

SOCS3 is essential for regulating the extent, duration, and specificity of cellular responses to cytokines such as G-CSF and IL-6. Here we describe the solution structure of SOCS3, the first structure determined for any SOCS protein, in complex with a phosphotyrosine-containing peptide from the IL-6 receptor signaling subunit gp130. The structure of the complex shows that seven peptide residues form a predominantly hydrophobic binding motif. Regions outside the SOCS3 SH2 domain are important for ligand binding, in particular, a single 15 residue alpha helix immediately N-terminal to the SH2 domain makes direct contacts with the phosphotyrosine binding loop and, in part, determines its geometry. The SH2 domain itself is remarkable in that it contains a 35 residue unstructured PEST motif insertion that is not required for STAT inhibition. The PEST motif increases SOCS3 turnover and affects its degradation pathway, implying that it has an important regulatory role inside the cell.
机译:SOCS3对于调节细胞对诸如G-CSF和IL-6等细胞因子的反应的程度,持续时间和特异性至关重要。在这里,我们描述了SOCS3的溶液结构,这是针对任何SOCS蛋白确定的第一个结构,与来自IL-6受体信号亚基gp130的含磷酸酪氨酸的肽复合。该复合物的结构表明七个肽残基形成主要的疏水结合基序。 SOCS3 SH2结构域之外的区域对于配体结合非常重要,特别是,紧邻SH2结构域N端的15个残基的单个α螺旋与磷酸酪氨酸结合环直接接触,并部分决定其几何形状。 SH2结构域本身很引人注目,因为它包含STAT抑制不需要的35个残基的非结构化PEST基序插入。 PEST基序增加了SOCS3的转化并影响其降解途径,这表明它在细胞内具有重要的调节作用。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号