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Related Concept Videos

Factors Affecting Protein-Drug Binding: Drug-Related Factors01:18

Factors Affecting Protein-Drug Binding: Drug-Related Factors

Drug binding to proteins is a complex phenomenon influenced by various drug-related factors, each playing a significant role in the interaction between drugs and proteins within the body.
One crucial factor in drug-protein binding is the drug's lipophilicity or its affinity for fat. More lipophilic drugs tend to have higher binding extents. For example, highly lipophilic drugs like cloxacillin exhibit substantial protein binding, with as much as 95% of the drug binding to proteins. In contrast,...
Conserved Binding Sites01:49

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.
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 analyses the...
Conserved Binding Sites01:49

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.
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 analyses the...
Ligand Binding Sites02:40

Ligand Binding Sites

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...
Factors Affecting Protein-Drug Binding: Protein-Related Factors01:20

Factors Affecting Protein-Drug Binding: Protein-Related Factors

Drug binding to proteins is a key aspect of pharmacokinetics and can influence a drug's distribution, absorption, and elimination in the body. Several factors, including the drug's physiochemical properties, protein concentration, disease states, and the number of binding sites on the protein, influence this process.
The physicochemical properties of a drug play a significant role in its ability to bind to proteins. Lipophilic drugs, which dissolve in fats, oils, and lipids, can be bound by...
Dose-Response Relationship: Selectivity and Specificity01:25

Dose-Response Relationship: Selectivity and Specificity

Drugs exert their therapeutic effects by interacting with receptors, enzymes, or ion channels that are present throughout the human body. The strength and duration of the interaction between a drug and its target receptor are characterized by the selectivity and specificity of the drug. Selectivity refers to a drug's strong preference for its intended target over other targets. For instance, isoprenaline, a non-selective β-adrenergic agonist, interacts with both β1- and β2-adrenergic receptors...

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Updated: Jun 6, 2026

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
06:50

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

Protein binding specificity versus promiscuity.

Gideon Schreiber1, Amy E Keating

  • 1Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel. gideon.schreiber@weizmann.ac.il

Current Opinion in Structural Biology
|November 13, 2010
PubMed
Summary
This summary is machine-generated.

This review explores protein binding specificity, explaining how proteins achieve selective or promiscuous interactions. It highlights molecular mechanisms and evolutionary strategies that govern these crucial biological relationships.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Structural Biology

Background:

  • Protein-protein interactions are fundamental to all biological processes, including information transfer, regulation, and cellular structure assembly.
  • Cellular environments feature low concentrations of specific binding partners but high concentrations of other macromolecules, enabling significant roles for weak, non-specific interactions.
  • Understanding protein binding specificity is key to deciphering cellular function and dysfunction.

Purpose of the Study:

  • To investigate the molecular and structural basis differentiating specific (monogamous) from promiscuous (polygamous) protein interactions.
  • To review recent research on how proteins achieve binding specificity or promiscuity.
  • To explore the functional implications of protein binding promiscuity, particularly in protein-protein interaction networks.

Main Methods:

  • Review of existing literature and research findings on protein-protein interactions.
  • Analysis of molecular and structural data to understand binding interfaces and mechanisms.
  • Examination of evolutionary selection principles (positive and negative selection) influencing binding specificity.

Main Results:

  • Multiple distinct molecular solutions can lead to binding through similar protein interfaces.
  • Protein specificity can be modulated by factors such as residue variation, conformational flexibility, and post-translational modifications.
  • Natively unstructured proteins, which gain structure upon binding, often act as hubs in interaction networks, demonstrating the functional importance of promiscuity.

Conclusions:

  • Protein binding specificity is achieved through diverse molecular strategies, allowing for both highly selective and broadly interactive proteins.
  • Conformational plasticity, varied binding residues, and post-translational modifications are key mechanisms for tuning protein interactions.
  • Promiscuous binding, especially via natively unstructured proteins, plays a critical role in complex biological systems and protein interaction networks.