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Related Concept Videos

Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

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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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G protein-coupled receptor (GPCR) signaling plays a crucial role in cell functioning. GPCR desensitization is an equally essential process. It allows cells to respond to changing environments and regain sensitivity to new stimuli while preventing unnecessary stimulation when no longer needed. Prolonged exposure to stimuli leads to GPCR desensitization. It involves blocking the receptors from binding and activating additional G proteins. This inhibits activation of downstream effectors, thereby...
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Conserved Binding Sites

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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.
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Pull-down of Calmodulin-binding Proteins
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Conformational frustration in calmodulin-target recognition.

Swarnendu Tripathi1, Qian Wang, Pengzhi Zhang

  • 1Department of Physics, University of Houston, Houston, TX, 77204, USA; Center for Theoretical Biological Physics, Rice University, Houston, TX, 77005, USA.

Journal of Molecular Recognition : JMR
|January 28, 2015
PubMed
Summary
This summary is machine-generated.

Calmodulin (CaM) uses distinct binding routes to interact with CaMKI and CaMKII kinases. This binding frustration, influenced by CaM domain contacts, affects protein recognition kinetics.

Keywords:
binding frustrationbinding route analysiscalmodulincalmodulin-binding targetscoarse-grained molecular simulationsprotein-protein associationtarget recognition

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • Calmodulin (CaM) is a crucial calcium-signaling protein.
  • CaM activates diverse Ca(2+)-dependent protein kinases.

Purpose of the Study:

  • To investigate the molecular mechanisms of CaM target recognition.
  • To compare CaM binding to CaMKI and CaMKII peptides.

Main Methods:

  • Experimentally constrained molecular simulations.
  • Detailed binding route analysis.

Main Results:

  • CaM target peptides exhibit distinct binding routes.
  • CaM-CaMKII complex shows higher binding frustration than CaM-CaMKI.
  • Binding frustration originates from C-domain to N-domain contact transitions in CaM.

Conclusions:

  • Binding frustration is a key factor in CaM-protein recognition kinetics.
  • Intermolecular contacts dictate the dynamics of CaM target binding.