灵活的铁:铁组中的障碍使蛋白质结构和功能有序
Vladimir N Uversky1,2, Gloria C Ferreira1,3,4
1Department of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL, United States.
Frontiers in molecular biosciences
|June 16, 2025
概括
这项研究表明,包括铁结合蛋白在内的人类铁组表现出显著的功能内在障碍. 这种疾病对蛋白质相互作用,修饰和细胞组织至关重要.
科学领域:
- 生物化学 生化学
- 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:
- 铁对于许多生物过程至关重要,主要在血红蛋白中用于运输氧气.
- 铁依赖酶占人类酶的很大一部分,强调了铁的代谢重要性.
- 人体铁体,包括各种铁结合蛋白质,在细胞功能中起着至关重要的作用.
研究的目的:
- 调查人类体内的内在障碍的患病率和功能意义.
- 弥合关于内在无序区域在铁结合蛋白中的作用的知识差距.
- 分析内在障碍对人体机体功能功能的贡献.
主要方法:
- 人体铁素组的生物信息分析.
- 对铁结合蛋白中内在无序区域的评估.
- 评估蛋白质与蛋白质相互作用,翻译后修改和液体与液体相分离的内在障碍的功能影响.
主要成果:
- 人类铁组包含大量的功能内在障碍.
- 在各种类型的铁结合蛋白中,内在无序的区域普遍存在.
- 铁体中的功能内在障碍与蛋白质-蛋白质相互作用,翻译后修改和液体-液体相分离有关.
结论:
- 内在障碍是人类铁体的一个重要特征,有助于其多样化的功能.
- 了解铁结合蛋白的内在障碍对于理解细胞过程至关重要.
- 这些发现为铁相关蛋白质的结构灵活性和功能适应性提供了见解.
相关概念视频
Translation
15.7K
Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
Translation Produces the Building Blocks of Life
Proteins are...
Translation Produces the Building Blocks of Life
Proteins are...
15.7K
Intrinsically Disordered Proteins
18.3K
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...
18.3K
Protein Modifications in the RER
5.7K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
5.7K
Regulation of Nuclear Protein Sorting
2.4K
Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
2.4K
Disorders of Erythrocytes
1.3K
Disorders of erythrocytes, or red blood cells (RBCs), include a range of conditions affecting their number, shape, or function.
Erythrocyte disorders can be broadly categorized into two main types: anemic and polycythemic conditions.
A low oxygen-carrying capacity of the blood due to the loss, lower production, or destruction of erythrocytes is termed anemia. Hemorrhagic anemia, for example, occurs when bleeding from an external wound or internal ulcer reduces erythrocyte counts.
On the other...
Erythrocyte disorders can be broadly categorized into two main types: anemic and polycythemic conditions.
A low oxygen-carrying capacity of the blood due to the loss, lower production, or destruction of erythrocytes is termed anemia. Hemorrhagic anemia, for example, occurs when bleeding from an external wound or internal ulcer reduces erythrocyte counts.
On the other...
1.3K
Regulation of the Unfolded Protein Response
2.6K
Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
2.6K


