相关实验视频
Updated: May 1, 2026

04:41
Measuring Lactase Enzymatic Activity in the Teaching Lab
Published on: August 6, 2018
117.2K
通过蛋白质内在障碍调节全ostery
Allan Chris M Ferreon1, Josephine C Ferreon, Peter E Wright
1Department of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.
Nature
|June 21, 2013
概括
在内在无序的蛋白质中,如腺病毒 E1A coprotein 中,Allostery 呈现出一种合作性开关. 这种机制微调蛋白相互作用和下游信号,这对于细胞调节至关重要.
科学领域:
- 生物化学和分子生物学
- 蛋白质动力学和阿洛斯特里
- 本质上有障碍的蛋白质 (IDP)
背景情况:
- 菌对球状蛋白质的细胞调节至关重要,并且越来越多地在内在无序蛋白质 (IDP) 中被识别出来.
- IDPs通常是分子中心,与多个合作伙伴相互作用,以腺病毒早期区域1A (E1A) oncoprotein为例.
- E1A与CREB结合蛋白 (CBP),p300和视网膜母细胞蛋白 (pRb) 等宿主调节剂相互作用,以重编程细胞.
研究的目的:
- 为了研究三元E1A-CBP-pRb系统中的全效应.
- 了解内在无序的蛋白相互作用网络中的合结合和折叠过程.
- 阐明合作在调节E1A复杂形成和下游信号传输中的作用.
主要方法:
- 使用单分子光共振能量转移 (smFRET) 来研究结合和折叠动态.
- 使用低蛋白度来控制E1A的聚合倾向和高亲和相互作用.
- 分析了三元E1A系统,观察了绑定事件中的合作性.
主要成果:
- 证明E1A-CBP-pRb相互作用表现出正或负的合作性,取决于可用的E1A结合点.
- 揭示了一种合作开关,可以微调三元复合体与二元E1A复合体的热力学可访问性.
- 表明这种调制允许下游信号输出对特定环境进行调.
结论:
- 像E1A这样的核心内在无序蛋白质中的Allosteric相互作用的特点是可调节的合作性开关.
- 这种开关机制对于调节蛋白质复合体形成和细胞通路下游信号传递至关重要.
- 表明这种全调制是内在无序的蛋白质枢纽的常见功能机制.
相关概念视频
Allosteric Regulation
53.3K
Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
53.3K
Allosteric Proteins-ATCase
4.8K
Binding sites linkages can regulate a protein's function. For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
4.8K
Overview of Protein Metabolism
4.5K
Proteins are broken down into amino acids during digestion. Unlike fats and carbohydrates, which are stored for later use, proteins are not. Instead, amino acids are either used to produce ATP through oxidation or contribute to the creation of new proteins for the growth and repair of the body. Any surplus amino acids from the diet are converted into glucose or triglycerides rather than excreted.
Amino acids play various roles in the body once they are absorbed into cells. They are restructured...
Amino acids play various roles in the body once they are absorbed into cells. They are restructured...
4.5K
Inborn Errors of Metabolism
1.1K
Phenylketonuria (PKU) is a protein metabolism disorder characterized by high blood levels of the amino acid phenylalanine. This results from a mutation in the gene responsible for phenylalanine hydroxylase, an enzyme that converts phenylalanine into tyrosine. When this enzyme is deficient, phenylalanine builds up in the blood, leading to symptoms such as vomiting, rashes, seizures, growth deficiency, and severe mental retardation. An early diagnosis and a diet restricting phenylalanine intake...
1.1K
Amino Acid Catabolism
1.7K
Microorganisms rely on proteins as an essential carbon and energy source, particularly in environments with limited polysaccharides or lipids. However, proteins are too large to cross the plasma membrane unaided, necessitating enzymatic degradation. Microbes secrete extracellular proteases and peptidases that hydrolyze proteins into peptides, which can then be transported across the membrane. Once inside the cell, intracellular proteases degrade these peptides into free amino acids, which...
1.7K
Amino Acid Biosynthetic Pathways
1.8K
Amino acid biosynthesis is essential for cell growth, protein synthesis, and metabolic regulation. Cells generate essential and non-essential amino acids from metabolic intermediates to sustain vital biological functions. These intermediates originate from key metabolic pathways: glycolysis, the tricarboxylic acid (TCA) cycle, and the pentose phosphate pathway. Important precursors include α-ketoglutarate, pyruvate, oxaloacetate, phosphoenolpyruvate, and erythrose-4-phosphate, which...
1.8K

