内部形状平衡位置的阿雷斯-2用于激活
bioRxiv : the preprint server for biology
|January 9, 2026
概括
在绑定合作伙伴之前,Arrestin-2本质上样本激活准备状态. 这项研究定义了控制预激活和信号能力的解决方案状态平衡.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 结构生物学 结构生物学
背景情况:
- 阿雷斯调节G蛋白合受体 (GPCR) 通过构造变化传递信号.
- 在预激活中控制arrest的溶液状态平衡并未得到充分理解.
研究的目的:
- 描述溶液中全长人体arrestin-2的内在形状景观.
- 为了定义在预激活中底层的解决方案状态平衡.
主要方法:
- 甲基特异性核磁共振 (NMR) 光谱. 甲基特异性核磁共振 (NMR) 光谱.
- 温度依赖的化学转移分析.
- 放松测量.放松的测量.
主要成果:
- 确定了两种不同的平衡,具有可分离的热力学和动力学特征.
- 在生理温度下,一个缓慢的,受热量影响的过程会在生理温度下形成一个类似活体的形状.
- 更快的平衡涉及C端尾部释放与相反的热力学行为.
结论:
- 阿雷斯-2 本质上样本激活相关的形状,没有结合伙伴.
- 提供了一个解决方案状态框架,用于阻止预先激活和信号能力.
相关概念视频
Activation and Inactivation of G Proteins
10.8K
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...
10.8K
Assembly of Signaling Complexes
6.5K
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,...
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
6.5K
The Two-State Receptor Model
3.0K
The two-state receptor model explains a drug's interaction with receptors, such as G protein-coupled receptors and ligand-gated ion channels, to induce or inhibit a biological response. When no natural ligands are present, a receptor exists in an equilibrium of inactive (Ri) and active (Ra) conformations. The inactive form does not produce a response, while the active form generates a basal effect known as constitutive activity.
The binding affinity of a drug determines its interaction with...
The binding affinity of a drug determines its interaction with...
3.0K
Generation of Straight or Branched Actin Filaments
3.7K
The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
3.7K
Calmodulin-dependent Signaling
6.0K
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
6.0K
ATP Synthase: Structure
15.1K
ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
15.1K


