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Updated: Jun 30, 2025

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
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对不同的对接协议进行基准测试,以预测与环氧酶酶复合的连接体的结合姿势,并选化学库

Sara Shamsian1,2, Babak Sokouti3, Siavoush Dastmalchi2,3,4

  • 1Student Research Committee, Tabriz University of Medical Sciences, Tabriz, 5165665931, ‎Iran.

BioImpacts : BI
|March 20, 2024
PubMed
概括

选择正确的分子对接程序对于发现新的抗炎药物至关重要. 格莱德在预测循环氧化酶 (COX) 酶的结合姿势方面表现出卓越的表现,有助于药物发现.

关键词:
药物发现 药物发现分子对接是分子对接.非类固醇抗炎药物 非类固醇抗炎药物在ROC分析中,ROC分析

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相关概念视频

The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
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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.
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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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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.
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Determining protein-drug binding can be achieved through indirect and direct methods, each providing valuable insights into the interaction between proteins and drugs.
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