LVPocket:集成的3D全球-本地信息,以预测蛋白质结合口袋,并转移蛋白质结构分类的学习
Ruifeng Zhou1, Jing Fan1, Sishu Li1
1School of Science, China Pharmaceutical University, Nanjing, 210009, Jiangsu, People's Republic of China.
Journal of cheminformatics
|July 7, 2024
概括
一种新的深度学习方法LVPocket通过使用变压器编码器集成本地和全球结构信息来改善蛋白质结合口袋预测. 转移学习进一步提高了不同蛋白质折叠结构类的准确性.
科学领域:
- 计算生物学是一种计算生物学.
- 结构生物信息学 结构生物信息学
- 在蛋白质科学中的深度学习应用.
背景情况:
- 对于蛋白质结合口袋预测的传统深度学习方法通常会因为3D卷积而过度强调本地结构信息.
- 现有的方法可能会忽视关键的全球结构上下文,这对于准确的绑定地点识别至关重要.
- 蛋白质折叠结构类显著影响生物功能,需要定制的预测模型.
研究的目的:
- 开发一种新的深度学习模型,LVPocket,有效地整合了本地和全球蛋白质结构信息.
- 解决卷积神经网络在捕捉蛋白质结构中长距离依赖性的局限性.
- 研究蛋白质折叠结构类对结合口袋预测的影响,并应用转移学习来提高性能.
主要方法:
- 将变压器编码器集成到深度学习架构中,以捕捉全球蛋白质结构背景.
- 在sc-PDB数据集上训练的基线LVPocket模型的开发.
- 应用转移学习来微调四个不同的蛋白质折叠结构类的LVPocket模型.
主要成果:
- 与三个独立数据集的最先进方法相比,LVPocket在绑定口袋预测方面表现优越.
- 微调模型利用转移学习显示出比基线LVPocket模型更好的性能.
- 提出的方法有效地平衡了捕获本地和全球蛋白质结构信息.
结论:
- 通过协同利用本地和全球结构特征,LVPocket在蛋白质结合口袋预测方面取得了重大进展.
- 针对蛋白质折叠结构类量身定制的转移学习提高了预测准确性,突出了结构多样性的重要性.
- LVPocket方法为预测蛋白质结合口袋提供了一个强大的解决方案,克服了纯粹卷积方法的局限性.
更多相关视频
06:50Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
Published on: January 26, 2024
1.8K
10:21Author Spotlight: Streamlining Protein Target Prediction and Validation via Molecular Docking and CETSA
Published on: February 23, 2024
2.5K
相关概念视频
Conserved Binding Sites
4.2K
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...
4.2K
Protein Organization
6.4K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
The primary structure of a protein is its amino acid sequence....
6.4K
Protein-protein Interfaces
12.5K
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...
12.5K
Protein and Protein Structure
79.4K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
A protein's shape is critical to its function. For example, an enzyme...
79.4K
Conservation of Protein Domains Over Different Proteins
10.8K
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...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
10.8K
Protein and Protein Structures
10.4K
10.4K
