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Related Concept Videos

Structure of Cadherins01:25

Structure of Cadherins

The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...
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...
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...
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
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Related Experiment Video

Updated: Jun 16, 2026

Monitoring ER/SR Calcium Release with the Targeted Ca2+ Sensor CatchER+
12:30

Monitoring ER/SR Calcium Release with the Targeted Ca2+ Sensor CatchER+

Published on: May 19, 2017

Structural diversity of calcium binding sites.

Daniel Bindreither1, Peter Lackner

  • 1Department of Molecular Biology, University of Salzburg, 5020 Salzburg, Austria.

General Physiology and Biophysics
|January 23, 2010
PubMed
Summary

Calcium Binding Proteins (CBPs) with known 3D structures are diverse. Their calcium (Ca2+) binding sites often involve distant amino acids and water molecules, not just continuous sequences.

Area of Science:

  • Structural Biology
  • Biochemistry
  • Bioinformatics

Background:

  • Calcium Binding Proteins (CBPs) are crucial for numerous biological functions.
  • Understanding the 3D structures of CBPs is key to elucidating their mechanisms.

Purpose of the Study:

  • To compile and analyze the 3D structures of Calcium Binding Proteins.
  • To characterize the structural features of calcium ion binding sites in CBPs.

Main Methods:

  • Data compilation from multiple structural databases.
  • Analysis of resolved 3D structures of Calcium Binding Proteins using X-ray crystallography and NMR data.
  • Bioinformatic analysis of protein folds, functional families, and calcium binding site characteristics.

Main Results:

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Membrane Remodeling of Giant Vesicles in Response to Localized Calcium Ion Gradients

Published on: July 16, 2018

Pull-down of Calmodulin-binding Proteins
07:51

Pull-down of Calmodulin-binding Proteins

Published on: January 23, 2012

Related Experiment Videos

Last Updated: Jun 16, 2026

Monitoring ER/SR Calcium Release with the Targeted Ca2+ Sensor CatchER+
12:30

Monitoring ER/SR Calcium Release with the Targeted Ca2+ Sensor CatchER+

Published on: May 19, 2017

Membrane Remodeling of Giant Vesicles in Response to Localized Calcium Ion Gradients
08:15

Membrane Remodeling of Giant Vesicles in Response to Localized Calcium Ion Gradients

Published on: July 16, 2018

Pull-down of Calmodulin-binding Proteins
07:51

Pull-down of Calmodulin-binding Proteins

Published on: January 23, 2012

  • CBP structures are highly diverse, spanning various functional families and fold types.
  • Calcium binding sites are often formed by residues from different secondary structure elements, not a continuous sequence.
  • Aspartic acid and Glutamic acid side chains are primary Ca(2+) interactors, with contributions from other residues and water molecules.

Conclusions:

  • The structural diversity of CBPs reflects their varied biological roles.
  • Calcium coordination in CBPs is a complex, often non-contiguous interaction involving multiple structural elements and water.