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相关概念视频

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Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high...
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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
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Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
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The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors...
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G Protein–Coupled Receptors (GPCRs) are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to various stimuli. GPCRs regulate critical physiological pathways and are excellent drug targets for treating diseases such as diabetes, cancer, obesity, depression, or Alzheimer's. Nearly 35% of approved drugs implement their therapeutic effects by selectively interacting with specific GPCRs.
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FGF受体二分化和激活的结构基础

A N Plotnikov1, J Schlessinger, S R Hubbard

  • 1Department of Pharmacology, New York University School of Medicine, New York 10016, USA.

Cell
|September 18, 1999
PubMed
概括
此摘要是机器生成的。

晶体结构揭示了纤维细胞生长因子2 (FGF2) 如何与纤维细胞生长因子受体1 (FGFR1) 结合,形成二分体. 这种结构解释了FGF和肝素诱导的受体二分化.

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科学领域:

  • 结构生物学 结构生物学
  • 生物化学 生物化学
  • 分子生物学分子生物学

背景情况:

  • 纤维细胞生长因子2 (FGF2) 对于细胞信号传递至关重要.
  • 纤维细胞生长因子受体1 (FGFR1) 中介FGF2信号传递.
  • 了解FGF2-FGFR1相互作用是解读细胞生长和分化途径的关键.

研究的目的:

  • 确定FGF2结合FGFR1.3的免疫球蛋白类域2和3 (D2和D3) 的晶体结构.
  • 阐明FGF2-FGFR1复合体形成和二元化背后的分子机制.
  • 为FGFR和肝素诱导的FGFR二元化提供结构基础.

主要方法:

  • 在2.8A分辨率的X射线晶体学.
  • 对FGF2:FGFR1复杂结构的分析.
  • 识别相互作用接口和潜在的肝素结合部位.

主要成果:

  • 晶体结构显示了由两个FGF2:FGFR1复合体形成的双重对称二元体.
  • FGF2与FGFR1域D2和D3以及域间链接器广泛相互作用.
  • 在FGFR1上,一个带正电的峡谷被确定为潜在的肝素结合部位.
  • 模态稳定涉及FGF2,D2域和互受体D2-D2接触之间的相互作用.

结论:

  • 晶体结构提供了FGF2-FGFR1复合物的详细分子模型.
  • 这些发现提供了关于FGF和氨酸介导的FGFR二分化机制的见解.
  • 这种结构性理解统一了现有的生化数据,并支持了受体激活的一般模型.