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相关概念视频

Conserved Binding Sites01:49

Conserved Binding Sites

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
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General Transcription Factors01:30

General Transcription Factors

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Tissue-specific transcription factors contribute to diverse cellular functions in mammals. For example, the gene for beta globin, a major component of hemoglobin, is present in all cells of the body. However, it is only expressed in red blood cells because the transcription factors that can bind to the promoter sequences of the beta globin gene are only expressed in these cells. Tissue-specific transcription factors also ensure that mutations in these factors may impair only the function of...
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Protein-protein Interfaces02:04

Protein-protein Interfaces

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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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...
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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
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Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

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Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
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相关实验视频

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Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
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Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

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对于TFIIS和Paf1C之间的进化保守相互作用的结构基础.

Jie Gao1, Miki Jishage2, Yuzhu Wang3

  • 1MOE Key Laboratory for Membraneless Organelles and Cellular Dynamics, Hefei National Research Center for Interdisciplinary Sciences at the Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230022, PR China; Department of Ophthalmology, The Second Affiliated Hospital of Anhui Medical University, 678 Furong Road, Hefei, Anhui, PR China.

International journal of biological macromolecules
|September 11, 2023
PubMed
概括
此摘要是机器生成的。

转录因子TFIIS在Paf1C复合体内与Leo1结合,这对RNA聚合酶II转录至关重要. 结构研究揭示了特定物种的相互作用,突出了转录调节的进化变异.

关键词:
在 LW 域名中,使用 LW 域名.莱昂1 莱昂1 莱昂1一个复杂的Paf1C复合体.蛋白质结构 蛋白质结构这是一个很好的例子. TFIIS转录条例 转录条例 转录条例 转录条例

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A High Resolution Method to Monitor Phosphorylation-dependent Activation of IRF3
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A High Resolution Method to Monitor Phosphorylation-dependent Activation of IRF3
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High Sensitivity Measurement of Transcription Factor-DNA Binding Affinities by Competitive Titration Using Fluorescence Microscopy
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科学领域:

  • 分子生物学分子生物学
  • 结构生物学 结构生物学
  • 进化生物学 进化生物学

背景情况:

  • 转录延长因子TFIIS与Paf1复合体 (Paf1C) 相互作用,通过RNA聚合酶II (Pol II) 促进过程性转录.
  • 了解TFIIS-Paf1C相互作用的结构基础是阐明转录调节机制的关键.

研究的目的:

  • 为了确定TFIIS LW域的晶体结构,与Trypanosoma的Leo1 LFG基因复合.
  • 阐明TFIIS-Paf1C相互作用的结构基础及其特定物种的变异.

主要方法:

  • 使用X射线晶体学来确定TFIIS LW域 (apo和复杂形式) 从Trypanosoma,酵母和人类的结构.
  • 结构分析的重点是保存的疏水核和TFIIS LW域在Leo1结合时的构造变化.

主要成果:

  • 保存的疏水核调解TFIIS LW域与Leo1跨物种的相互作用.
  • 结合Trypanosoma Leo1会在TFIIS LW域的α6螺旋中诱导独特的形状变化,这种变化在酵母和人类中不存在.
  • 这种形状差异解释了Trypanosoma的更高的结合亲和力,并表明了特定物种的相互作用变化.

结论:

  • 与Leo1的LFG动机的TFIIS LW域相互作用对于定Paf1C复合体至关重要.
  • 这些发现为TFIIS-Paf1C相互作用提供了详细的结构基础,并阐明了这些因素对转录调节的演变.