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Activation and Inactivation of G Proteins01:22

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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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Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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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
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
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Intracellular Signaling Affects Focal Adhesions01:17

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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.
Some...
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TGF - β Signaling Pathway01:16

TGF - β Signaling Pathway

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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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Transducer Mechanism: G Protein–Coupled Receptors01:30

Transducer Mechanism: G Protein–Coupled 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.
GPCRs are also called heptahelical,...
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G Protein-coupled Receptors01:15

G Protein-coupled Receptors

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G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
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FGF受容体のダイメリゼーションと活性化の構造的基礎

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
まとめ
この要約は機械生成です。

結晶構造は,ファイブロブラスト成長因子2 (FGF2) が,ファイブロブラスト成長因子受容体1 (FGFR1) に結合し,二重体を形成する方法を示しています. この構造は,FGFおよびヘパリン誘発の受容体二分化を説明する.

さらに関連する動画

Oligomerization Dynamics of Cell Surface Receptors in Living Cells by Total Internal Reflection Fluorescence Microscopy Combined with Number and Brightness Analysis
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Studying the Stoichiometry of Epidermal Growth Factor Receptor in Intact Cells using Correlative Microscopy
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Oligomerization Dynamics of Cell Surface Receptors in Living Cells by Total Internal Reflection Fluorescence Microscopy Combined with Number and Brightness Analysis
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Studying the Stoichiometry of Epidermal Growth Factor Receptor in Intact Cells using Correlative Microscopy
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科学分野:

  • 構造生物学 構造生物学とは
  • バイオケミストリー バイオケミストリー
  • 分子生物学は分子生物学である.

背景:

  • フィブロブラスト成長因子2 (FGF2) は,細胞シグナル伝達に不可欠です.
  • 線維細胞成長因子受容体1 (FGFR1) は,FGF2の信号伝達を媒介する.
  • FGF2-FGFR1の相互作用を理解することは,細胞成長と分化経路の解読の鍵です.

研究 の 目的:

  • FGFR1.1の免疫グロブリン類似ドメイン2と3 (D2とD3) に結合するFGF2の結晶構造を決定する.
  • FGF2-FGFR1複合体の形成と二分化の基礎となる分子メカニズムを解明する.
  • FGFRおよびヘパリン誘発のFGFR二分化に構造的基礎を提供するために.

主な方法:

  • 2.8Aの解像度のX線結晶学.
  • FGF2:FGFR1複合構造の分析. FGF2:FGFR1複合構造の分析. FGF2:FGFR1複合構造の分析. FGF2:FGFR1複合構造の分析. FGF2:FGFR1複合構造の分析.
  • 相互作用界面と潜在的なヘパリン結合部位の特定.

主要な成果:

  • 結晶構造は,2つのFGF2:FGFR1複合体によって形成された2倍対称な二重体を示しています.
  • FGF2は,FGFR1のドメインD2とD3と,ドメイン間のリンク器と広く相互作用する.
  • FGFR1の陽性電荷の峡谷は,潜在的なヘパリン結合部位として特定されています.
  • ディマー安定化には,FGF2,D2ドメイン,およびインターレセプターD2-D2コンタクトの間の相互作用が含まれます.

結論:

  • 結晶構造は,FGF2-FGFR1複合体の詳細な分子モデルを提供します.
  • この発見は,FGFおよびヘパリン媒介のFGFR二分化のメカニズムについての洞察を提供します.
  • この構造的な理解は,既存の生化学データを統合し,受容体活性化の一般的なモデルをサポートします.