相关实验视频
Updated: May 27, 2026

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Oligopeptide Competition Assay for Phosphorylation Site Determination
Published on: May 18, 2017
酸化位点进化的机制
Samuel M Pearlman1, Zach Serber, James E Ferrell
1Department of Chemical and Systems Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Cell
|November 15, 2011
概括
大自然从酸性残留物,如阿斯巴酸和谷氨酸酸,进化了蛋白质酸化部位. 这种进化策略解释了酸化如何激活蛋白质,并揭示了它的起源.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 进化生物学 进化生物学
背景情况:
- 蛋白质酸化是一种关键的调节机制,通过可逆添加基来控制蛋白质功能.
- 酸化引入负电荷,而酸性残留物 (酸盐/酸盐) 可以模仿这种状态.
- 酸化地点的进化起源尚未完全理解.
研究的目的:
- 为了研究蛋白质酸化场所的进化起源.
- 探索酸性残留物是否可以作为酸化场所的前体.
- 了解从酸性残留物中演变的酸化部位的功能影响.
主要方法:
- 比较基因组学方法来识别进化模式.
- 蛋白质的结构分析 (DNA topoisomerase II,enolase,C-Raf) 具有从酸性残留物进化的酸盐.
主要成果:
- 证明大自然从酸盐和谷氨酸盐残留物中演化出血清素,三素和氨酸酸化部位.
- 结构分析显示,盐与基本残留物的桥梁中有酸性残留物,酸化可以有条件地恢复这些残留物.
- 确定了特定的蛋白质 (DNA拓酶II,酶,C-Raf),以此为例,说明了这一进化途径.
结论:
- 从酸性残留物进化酸化位提供了条件蛋白激活的机制.
- 这一发现提供了一个解释为什么某些蛋白质被酸化激活的理由.
- 为了解蛋白质酸化的起源和复杂性做出贡献.
相关概念视频
Phosphorylation
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Phosphorylation
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Protein Kinases and Phosphatases
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein Kinases and Phosphatases
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Covalently Linked Protein Regulators
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.
These groups modify specific amino acids in a protein.
Amplifying Signals via Enzymatic Cascade
When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...
