不同的LARP1 PAM2图案采用了对MLLE结合的非正规形态
Ali Behvarmanesh1, Guennadi Kozlov1, Tara Sprules2
1Department of Biochemistry, McGill University, Montréal, Québec, H3G 0B1, Canada; Centre de Recherche en Biologie Structurale, McGill University, Montréal, Québec, H3G 0B1, Canada.
Biochemical and biophysical research communications
|February 28, 2026
概括
细胞质多A结合蛋白1 (PABPC1) 与La相关蛋白1 (LARP1) 通过非正规的动机相互作用. 这揭示了PABPC1如何使用的灵活性.
科学领域:
- 分子生物学分子生物学
- 蛋白相互作用 蛋白相互作用
- 在RNA代谢过程中.
背景情况:
- 细胞质多A结合蛋白1 (PABPC1) 通过RNA识别基因 (RRMs) 结合mRNA多A尾部.
- PABPC1的C端MLLE域招募含有PAM2基因的调节蛋白.
- 与La相关的蛋白1 (LARP1) 与PABPC1相互作用,但具有非典型的PAM2序列.
研究的目的:
- 阐明LARP1的PAM2动机与PABPC1的MLLE域之间的相互作用的分子基础.
- 描述涉及LARP1.1的非正规PAM2-MLLE相互作用.
主要方法:
- 核磁共振 (NMR) 光谱学 核磁共振 (NMR) 光谱学
- 异热定位热量计 (ITC) 是一种热量计.
- AlphaFold3 蛋白质结构建模模型
主要成果:
- 核磁共振确定了LARP1内负责MLLE结合的特定PAM2动图段.
- 突变和ITC证实Phenylalanine 496对于MLLE相互作用至关重要.
- AlphaFold3预测了LARP1 PAM2动机中的单转α螺旋.
结论:
- 定义了LARP1和PABPC1的MLLE域之间的非正规相互作用.
- 该研究强调了MLLE域识别PAM2图案的可塑性.
- 这些发现提升了对LARP蛋白质对mRNA代谢调节的理解.
相关概念视频
Conserved Binding Sites
5.2K
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...
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...
5.2K
Conserved Binding Sites
2.0K
2.0K
Ligand Binding Sites
15.4K
Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
15.4K
Ligand Binding Sites
9.0K
9.0K
Mechanism of Filopodia Formation
3.3K
Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
3.3K
Mechanism of Lamellipodia Formation
3.8K
Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
3.8K


