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Related Concept Videos

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:
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: 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,...

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Related Experiment Video

Updated: Jul 12, 2026

Purification of Human S100A12 and Its Ion-induced Oligomers for Immune Cell Stimulation
12:55

Purification of Human S100A12 and Its Ion-induced Oligomers for Immune Cell Stimulation

Published on: September 29, 2019

Theoretical study on binding of S100B protein.

Artur Gieldon1, Mattia Mori, Rebecca Del Conte

  • 1Protera S. r. l., Viale delle Idee, 22, 50019, Sesto Fiorentino, Fi, Italy. gieldon@proterasrl.com

Journal of Molecular Modeling
|August 24, 2007
PubMed
Summary

Researchers identified key residues on S100B protein essential for binding to tumor suppressor p53. This finding aids in developing new anti-cancer drugs by targeting S100B-p53 complexes.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Drug Discovery

Background:

  • S100B protein down-regulates tumor suppressor p53, a critical factor in cell cycle arrest and apoptosis.
  • Inactivation of p53 is implicated in over half of human cancers, making its restoration a therapeutic target.
  • Disrupting S100B-p53 complexes offers a potential strategy for anti-cancer drug development.

Purpose of the Study:

  • To elucidate the S100B binding interface for p53.
  • To identify specific residues involved in S100B-p53 complex formation.
  • To propose mechanisms for S100B ligand interactions, such as with pentamidine.

Main Methods:

  • Literature review to gather existing data on S100B and p53 interactions.
  • Molecular modeling (MM) techniques utilizing the AutoDock program.

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  • Application of the AMBER force field for computational analysis.

    • Main Results:

    • Identified four key residues (Val56, Phe76, Val52, Ala83) essential for S100B ligand binding.
    • Demonstrated that interactions with these residues are crucial for reducing S100B-p53 complex formation.
    • Proposed two distinct S100B-pentamidine complex structures and elucidated pentamidine's mechanism of action.

    Conclusions:

    • The identified S100B binding interface provides critical insights for anti-cancer drug design.
    • Targeting specific residues on S100B can disrupt the S100B-p53 complex, potentially restoring p53 function.
    • These findings facilitate the rational design of novel S100B ligands with therapeutic potential.