• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Molecular Biology >Lipid-binding hSH3 domains in immune cell adapter proteins.
【24h】

Lipid-binding hSH3 domains in immune cell adapter proteins.

机译：免疫细胞衔接蛋白中的脂质结合hSH3结构域。

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

SH3 domains represent versatile scaffolds within eukaryotic cells by targeting proline-rich sequences within intracellular proteins. More recently, binding of SH3 domains to unusual peptide motifs, folded proteins or lipids has been reported. Here we show that the newly defined hSH3 domains of immune cell adapter proteins bind lipid membranes with distinct affinities. The interaction of the hSH3 domains of adhesion and degranulation promoting adapter protein (ADAP) and PRAM-1 (Promyelocytic-Retinoic acid receptor alpha target gene encoding an Adaptor Molecule-1), with phosphatidylcholine-containing liposomes is observed upon incorporation of phosphatidylserine (PS) or phosphoinositides (PIs) into the membrane bilayer. Mechanistically we show that stable association of the N-terminal, amphipathic helix with the beta-sheet scaffold favours lipid binding and that the interaction with PI(4,5)P(2)-containing liposomes is consistent with a single-site, non-cooperative binding mechanism. Functional investigations indicate that deletion of both amphipathic helices of the hSH3 domains reduces the ability of ADAP to enhance adhesion and migration in stimulated T cells.
机译：SH3结构域通过靶向胞内蛋白内富含脯氨酸的序列来代表真核细胞内的多功能支架。最近，已经报道了SH3结构域与不寻常的肽基序，折叠的蛋白质或脂质的结合。在这里，我们显示免疫细胞衔接蛋白的新定义的hSH3域以不同的亲和力结合脂质膜。掺入磷脂酰丝氨酸（PS）后，观察到hSH3粘附和脱粒促进衔接蛋白（ADAP）和PRAM-1（早幼粒细胞-视黄酸受体α靶基因编码衔接分子-1）的结构域与含磷脂酰胆碱的脂质体之间的相互作用。 ）或磷酸肌醇（PIs）进入膜双层。从机理上讲，我们显示N末端两亲性螺旋与β-折叠支架的稳定缔合有利于脂质结合，并且与含PI（4,5）P（2）的脂质体的相互作用与单点，非-合作结合机制。功能研究表明，hSH3结构域的两个两亲性螺旋的缺失降低了ADAP增强刺激T细胞粘附和迁移的能力。

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