Calmodulin: Difference between revisions
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==Calmodulin== | |||
[[File:Calmodulin.png|Calmodulin|thumb|right]] | |||
Calmodulin | |||
'''Calmodulin''' (CaM) is a multifunctional intermediate calcium-binding messenger protein expressed in all eukaryotic cells. It is an essential component of the calcium signal transduction pathway, where it acts as a calcium sensor and signal transducer. Calmodulin is involved in a wide range of cellular processes, including muscle contraction, intracellular movement, cell division, and the regulation of metabolic pathways. | |||
Calmodulin | |||
== | ==Structure== | ||
Calmodulin is a small, highly conserved protein composed of 148 amino acids. It has a dumbbell-shaped structure with two globular domains connected by a flexible linker. Each domain contains two [[EF-hand]] motifs, which are helix-loop-helix structures that bind calcium ions. | |||
[[File:EFhandmotif.jpg|EF-hand motif|thumb|left]] | |||
===EF-hand Motifs=== | |||
The EF-hand motif is a common structural domain found in calcium-binding proteins. In calmodulin, each EF-hand can bind one calcium ion, allowing the protein to bind a total of four calcium ions. The binding of calcium induces a conformational change in calmodulin, enabling it to interact with various target proteins. | |||
==Function== | |||
Calmodulin functions as a calcium sensor and signal transducer. Upon binding calcium, calmodulin undergoes a conformational change that allows it to interact with and regulate a variety of target proteins, including kinases, phosphatases, ion channels, and other enzymes. | |||
===Calmodulin Binding Sites=== | |||
[[File:Calmodulin_Binding_sites.gif|Calmodulin binding sites|thumb|right]] | |||
Calmodulin interacts with its target proteins through specific binding sites. These sites are often characterized by a basic amphiphilic helix that fits into the hydrophobic pocket of calmodulin. The interaction is calcium-dependent, meaning that calmodulin must be bound to calcium to effectively bind its targets. | |||
==Role in Cellular Processes== | |||
Calmodulin plays a critical role in various cellular processes: | |||
* '''Muscle Contraction''': Calmodulin regulates muscle contraction by activating myosin light chain kinase (MLCK), which phosphorylates myosin light chains, facilitating interaction with actin filaments. | |||
[[File:Calmodulin_bound_to_MLC_Kinase.jpg|Calmodulin bound to MLC Kinase|thumb|left]] | |||
* '''Cell Cycle Regulation''': Calmodulin is involved in the regulation of the cell cycle by modulating the activity of various kinases and phosphatases. | |||
* '''Signal Transduction''': Calmodulin acts as a key mediator in calcium signal transduction pathways, influencing cellular responses to external stimuli. | |||
==Calmodulin in Plants== | |||
[[File:Sorghum_bicolor_(4171536532).jpg|Calmodulin in Sorghum bicolor|thumb|right]] | |||
In plants, calmodulin is involved in various physiological processes, including growth, development, and response to environmental stimuli. It plays a role in the regulation of plant-specific processes such as stomatal movement and gravitropism. | |||
==Calmodulin Domains== | |||
===N-terminal Domain=== | |||
[[File:Calmodulin_N-terminal.jpg|Calmodulin N-terminal|thumb|left]] | |||
The N-terminal domain of calmodulin contains two EF-hand motifs and is responsible for binding the first two calcium ions. This domain undergoes a conformational change upon calcium binding, which is crucial for its interaction with target proteins. | |||
===C-terminal Domain=== | |||
[[File:Calmodulin_C-terminal.jpg|Calmodulin C-terminal|thumb|right]] | |||
The C-terminal domain also contains two EF-hand motifs and binds the remaining two calcium ions. The C-terminal domain is important for the stability of the calcium-calmodulin complex and its interaction with target proteins. | |||
==Related Pages== | |||
* [[Calcium signaling]] | * [[Calcium signaling]] | ||
* [[ | * [[EF-hand]] | ||
* [[ | * [[Signal transduction]] | ||
* [[Muscle contraction]] | |||
{{Protein-stub}} | |||
[[Category:Calcium-binding proteins]] | |||
[[Category:Signal transduction]] | |||
[[Category:Proteins]] | [[Category:Proteins]] | ||
Latest revision as of 19:02, 23 March 2025
Calmodulin[edit]
Calmodulin (CaM) is a multifunctional intermediate calcium-binding messenger protein expressed in all eukaryotic cells. It is an essential component of the calcium signal transduction pathway, where it acts as a calcium sensor and signal transducer. Calmodulin is involved in a wide range of cellular processes, including muscle contraction, intracellular movement, cell division, and the regulation of metabolic pathways.
Structure[edit]
Calmodulin is a small, highly conserved protein composed of 148 amino acids. It has a dumbbell-shaped structure with two globular domains connected by a flexible linker. Each domain contains two EF-hand motifs, which are helix-loop-helix structures that bind calcium ions.
EF-hand Motifs[edit]
The EF-hand motif is a common structural domain found in calcium-binding proteins. In calmodulin, each EF-hand can bind one calcium ion, allowing the protein to bind a total of four calcium ions. The binding of calcium induces a conformational change in calmodulin, enabling it to interact with various target proteins.
Function[edit]
Calmodulin functions as a calcium sensor and signal transducer. Upon binding calcium, calmodulin undergoes a conformational change that allows it to interact with and regulate a variety of target proteins, including kinases, phosphatases, ion channels, and other enzymes.
Calmodulin Binding Sites[edit]
Calmodulin interacts with its target proteins through specific binding sites. These sites are often characterized by a basic amphiphilic helix that fits into the hydrophobic pocket of calmodulin. The interaction is calcium-dependent, meaning that calmodulin must be bound to calcium to effectively bind its targets.
Role in Cellular Processes[edit]
Calmodulin plays a critical role in various cellular processes:
- Muscle Contraction: Calmodulin regulates muscle contraction by activating myosin light chain kinase (MLCK), which phosphorylates myosin light chains, facilitating interaction with actin filaments.
- Cell Cycle Regulation: Calmodulin is involved in the regulation of the cell cycle by modulating the activity of various kinases and phosphatases.
- Signal Transduction: Calmodulin acts as a key mediator in calcium signal transduction pathways, influencing cellular responses to external stimuli.
Calmodulin in Plants[edit]
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In plants, calmodulin is involved in various physiological processes, including growth, development, and response to environmental stimuli. It plays a role in the regulation of plant-specific processes such as stomatal movement and gravitropism.
Calmodulin Domains[edit]
N-terminal Domain[edit]
The N-terminal domain of calmodulin contains two EF-hand motifs and is responsible for binding the first two calcium ions. This domain undergoes a conformational change upon calcium binding, which is crucial for its interaction with target proteins.
C-terminal Domain[edit]
The C-terminal domain also contains two EF-hand motifs and binds the remaining two calcium ions. The C-terminal domain is important for the stability of the calcium-calmodulin complex and its interaction with target proteins.
Related Pages[edit]
