在一个多域蛋白质中,域间移动性的模型
Yaroslav E Ryabov1, David Fushman
1Department of Chemistry and Biochemistry, Center for Biomolecular Structure and Organization, University of Maryland, College Park, Maryland 20742, USA.
Journal of the American Chemical Society
|February 27, 2007
概括
我们开发了一种新的NMR模型来研究蛋白质域的移动性. 该模型描述了Lys48结合的duibiquitin的结构和动态特性,揭示了对生物功能至关重要的域重定向.
科学领域:
- 生物物理学的生物物理.
- 结构生物学 结构生物学
- 生物化学 生物化学
背景情况:
- 蛋白质域的移动性对于生物功能至关重要.
- 核磁共振研究需要考虑域间运动以及其他动态.
- 与lys48结合的duibiquitin的功能受到域相互作用的影响.
研究的目的:
- 提出和验证一个新的模型,用于多域蛋白的域间移动性.
- 使用NMR来描述Lys48结合二维基因的结构和运动性质.
- 为了研究控制duibiquitin.conformational状态平衡的机制.
主要方法:
- 开发一种新模型,将域重定向纳入作为 conformational 交换和 anisotropic tumbling 的新模式.
- 在不同的pH值下对与lys48相关的duibiquitin进行15N放松数据的分析.
- 拟议模型与扩展型无模型方法的比较.
主要成果:
- 拟议的模型充分适应duibiquitin的实验NMR数据.
- 在9-30 ns的时间尺度上识别了域重定向,具有足够的幅度用于连接器访问.
- 建议His68的质子化作为控制duibiquitin构成状态之间的平衡的一个关键因素.
结论:
- 这种新型模型有效地描述了多域蛋白质的动态和结构性质.
- 迪乌比奎丁表现出对生物相互作用至关重要的形状灵活性.
- 这项研究提供了关于diubiquitin形状和功能的pH依赖调节的见解.
相关概念视频
Conservation of Protein Domains Over Different Proteins
Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Conservation of Protein Domains
Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Protein Diffusion in the Membrane
Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
Membrane Domains
The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...
Insertion of Multi-pass Transmembrane Proteins in the RER
The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
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Mechanisms of Membrane Domain Formation
Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...

