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Updated: Jan 15, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
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Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

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PPI-ID:通过域和SLiM映射简化蛋白质-蛋白质相互作用预测

Haley V Goodwin1,2, Nigel S Atkinson1,2

  • 1Department of Neuroscience, University of Texas at Austin, Austin, Texas, United States of America.

PLoS computational biology
|October 16, 2025
PubMed
概括

蛋白质-蛋白质相互作用标识符 (PPI-ID) 工具准确地将蛋白质相互作用域和图案映射到3D结构上. 它通过预测和过潜在的蛋白质-蛋白质相互作用 (PPI) 来增强蛋白质复杂模型.

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Conservation of Protein Domains Over Different Proteins

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Protein-protein Interfaces

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...
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Conserved Binding Sites

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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An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
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