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相关概念视频

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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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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Protein Folding01:22

Protein Folding

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Overview
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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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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
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Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
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核酸和蛋白质内内在无序区域之间的竞争.

Xi Wang1, Yaakov Levy2, Junji Iwahara1

  • 1Department of Biochemistry & Molecular Biology, Sealy Center for Structural Biology & Molecular Biophysics, University of Texas Medical Branch, Galveston, Texas 7755-1068, United States.

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概括

富含阿斯巴达酸 (D) 或谷氨酸 (E) 的蛋白质中负电荷的内在无序区域 (IDR) 比负电荷的区域更为常见. 这些IDR模仿核酸,影响DNA/RNA结合蛋白的功能和特异性.

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科学领域:

  • 生物化学 生物化学
  • 分子生物学分子生物学
  • 生物信息学是一种生物信息学.

背景情况:

  • 内在无序区域 (IDR) 对于蛋白质功能至关重要,电荷分布起着关键作用.
  • 许多蛋白质具有高度负电荷的IDR,富含亚斯巴酸盐 (D) 或谷氨酸酸盐 (E) 残留物.
  • 生物信息分析显示,负电荷的IDR比负电荷的IDR更为普遍.

研究的目的:

  • 探索负电荷IDRs的流行率和功能意义.
  • 了解这些区域如何与DNA结合域 (DBDs) 和RNA结合域 (RBDs) 相互作用.
  • 阐明负电荷的IDRs在蛋白质核酸相互作用和特异性的作用.

主要方法:

  • 蛋白质序列的生物信息分析,以识别带电残留道.
  • 关于内在无序区域的功能和调节的文献综述.
  • 分析IDRs和核酸之间的静电相互作用.

主要成果:

  • 在268个人类蛋白质中发现了10+个连续D/E残留的序列,而K/R只有12个.
  • 大约50%的具有D/E通道的蛋白质是DNA/RNA结合蛋白.
  • 负电荷的IDR可以模仿核酸,竞争结合点并影响蛋白质功能.

结论:

  • 负电荷的IDR不仅仅是抑制性的,而且积极增强DNA/RNA结合蛋白的功能.
  • 这些区域加快了目标搜索,从诱中拯救蛋白质,并增加了结合特异性.
  • 了解负电荷的IDR对于蛋白质工程和理解与突变相关的疾病机制至关重要.