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Calmodulin-dependent Signaling01:16

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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.
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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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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...
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Pull-down of Calmodulin-binding Proteins
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Conformational heterogeneity of the calmodulin binding interface.

Diwakar Shukla1,2,3, Ariana Peck4, Vijay S Pande1,2

  • 1Department of Chemistry, Stanford University, Stanford, California 94305, USA.

Nature Communications
|April 5, 2016
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Summary

Calmodulin (CaM) binding diversity is explained by distinct sub-states in its C-terminal domain, not unfolding. A novel Ca(2+)-bound interface offers therapeutic potential.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Computational Biology

Background:

  • Calmodulin (CaM) is a vital calcium sensor and signaling hub implicated in various diseases.
  • The molecular mechanisms underlying CaM's diverse binding interactions with proteins like GPCRs, ion channels, and kinases are not fully understood.

Purpose of the Study:

  • To elucidate the molecular basis of Calmodulin's diverse binding capabilities.
  • To investigate the role of conformational states and Ca(2+) in CaM binding specificity.

Main Methods:

  • Utilized high-resolution molecular dynamics simulations.
  • Applied Markov state models to analyze CaM's conformational landscape.
  • Developed a computational model to dissect CaM binding mechanisms.

Main Results:

  • Identified distinct sub-states in the CaM C-terminal domain (apo-CaM) that present unique chemical and steric features, supporting conformational selection.
  • Demonstrated that local unfolding is not the primary pathway for peptide binding in CaM.
  • Predicted a novel binding interface in the Ca(2+)-bound state of CaM.

Conclusions:

  • CaM's binding diversity arises from pre-existing sub-states in its apo form, rather than unfolding.
  • The identified Ca(2+)-bound interface represents a potential target for developing CaM-based therapeutics.