Sandbox 4465: Difference between revisions
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Its importance can be exemplified by the fact that the protein has been known to be highly conserved in eukaryotes. Highly conserved structures that do not undergo significant evolutionary changes imply that the structure is mandatory for cell or organism survival and that any mutations in the genetic sequence that codes for the protein would be deleterious. The function of calmodulin is typically studied using yeast as a model organism. This is done for a variety of reasons, including the fact that yeast has a fully annotated genome with human homologues for genes associated with their ion channels, yeast is fast growing and they are heat stable<ref>Wolfe, D. M. D. M. (2006). Channeling studies in yeast: Yeast as a model for channelopathies?</ref>. | Its importance can be exemplified by the fact that the protein has been known to be highly conserved in eukaryotes. Highly conserved structures that do not undergo significant evolutionary changes imply that the structure is mandatory for cell or organism survival and that any mutations in the genetic sequence that codes for the protein would be deleterious. The function of calmodulin is typically studied using yeast as a model organism. This is done for a variety of reasons, including the fact that yeast has a fully annotated genome with human homologues for genes associated with their ion channels, yeast is fast growing and they are heat stable<ref>Wolfe, D. M. D. M. (2006). Channeling studies in yeast: Yeast as a model for channelopathies?</ref>. | ||
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== Function == | == Function == | ||
Each end of the globular domains of CaM binds to two Calcium ions, which allows CaM to bind to a total of four Calcium ions. The conformational changes which CaM undergoes allow it to be able to bind more specifically. Calmodulin elicits a pathway signal transduction by activating protein kinases which can then go on to phosphorylate other proteins, or other proteins can directly bind to Calmodulin. This would require that the other proteins have a specific binding motif or substrate binding mechanism for Calmodulin. Because there are many different types of binding motifs used by other proteins to interact with Calmodulin, there are no conserved amino acid sequences for CaM binding. | Each end of the globular domains of CaM binds to two Calcium ions, which allows CaM to bind to a total of four Calcium ions. The conformational changes which CaM undergoes allow it to be able to bind more specifically. Calmodulin elicits a pathway signal transduction by activating protein kinases which can then go on to phosphorylate other proteins, or other proteins can directly bind to Calmodulin<ref>doi:10.1128/EC.01.1.119-125.2002</ref>. This would require that the other proteins have a specific binding motif or substrate binding mechanism for Calmodulin. Because there are many different types of binding motifs used by other proteins to interact with Calmodulin, there are no conserved amino acid sequences for CaM binding. | ||
Some functions of calmodulin are associated with apoptosis, inflammation, metabolism, and smooth muscle contraction<ref>doi:10.1074/jbc.M111.336032</ref>. Based on a study done on Drosophila neuronal cells, calmodulin plays a role in the apoptotic pathways<ref>Ui-Tei, K., Nagano, M., Sato, S., & Miyata, Y. (2000). Calmodulin-dependent and -independent apoptosis in cell of a drosophila neuronal cell line</ref>. | |||
</StructureSection> | </StructureSection> | ||
== Bibliography == | == Bibliography == | ||
<references/> | <references/> | ||
