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Related Concept Videos

Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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 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,...
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...
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Factors Affecting Protein-Drug Binding: Drug Interactions01:23

Factors Affecting Protein-Drug Binding: Drug Interactions

Drug interactions are a critical aspect of pharmacology and can occur when two or more drugs compete for the same binding site. This competition can result in one drug displacing another, altering the effect of the displaced drug. Drug interactions are complex processes that rely heavily on how much of the displacer drug is present and how strongly it can bind to the same sites as the displaced drug.
Displacement interactions can have varying outcomes, ranging from toxicity to virtually...

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Related Experiment Video

Updated: Jul 3, 2026

Pull-down of Calmodulin-binding Proteins
07:51

Pull-down of Calmodulin-binding Proteins

Published on: January 23, 2012

Structural differences between Pb2+- and Ca2+-binding sites in proteins: implications with respect to toxicity.

Michael Kirberger1, Jenny J Yang

  • 1Center for Drug Design and Biotechnology, Department of Chemistry, Georgia State University, 50 Decatur Street, 550 NSC, Atlanta, GA 30303, USA.

Journal of Inorganic Biochemistry
|August 8, 2008
PubMed
Summary

Lead (Pb2+) ions can displace essential metal ions in proteins, potentially causing toxicity. This study found lead binds to diverse protein sites, suggesting opportunistic binding contributes to its molecular toxicity.

Related Experiment Videos

Last Updated: Jul 3, 2026

Pull-down of Calmodulin-binding Proteins
07:51

Pull-down of Calmodulin-binding Proteins

Published on: January 23, 2012

Area of Science:

  • Biochemistry
  • Toxicology
  • Structural Biology

Background:

  • Lead (Pb2+) ions are known to interfere with essential metal ions in biological systems.
  • Understanding Pb2+ interactions with proteins is crucial for elucidating its toxicity mechanisms.

Purpose of the Study:

  • To compare the structural characteristics of Pb2+-binding sites with calcium (Ca2+)-binding sites in proteins.
  • To investigate the structural consequences of Pb2+ binding in specific proteins like calmodulin (CaM) and 5-aminolaevulinic acid dehydratase (ALAD).

Main Methods:

  • Analysis of data from the Protein Data Bank (PDB).
  • Comparison of ligand count, net negative charge, and dominant ligand types for Pb2+ and Ca2+ binding sites.
  • Examination of protein structural changes upon Pb2+ or Ca2+ displacement in CaM and ALAD.

Main Results:

  • Pb2+ binding sites typically have fewer ligands (2-5) compared to Ca2+ sites (EF-Hand: 7±1, non-EF-Hand: 6±2).
  • Glutamate (Glu) is a predominant ligand for Pb2+ (38.4%), more so than for Ca2+ sites.
  • Pb2+ binding induced structural changes in CaM and ALAD, suggesting adaptation and opportunistic binding rather than simple ionic displacement.

Conclusions:

  • Pb2+ exhibits adaptability to various binding geometries within proteins.
  • Opportunistic binding of Pb2+ to proteins, particularly in charged regions or active sites, likely contributes significantly to molecular toxicity.