Sandbox 4465

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==Calmodulin==
==Calmodulin==
<StructureSection load='2bcx' size='340' side='right' caption='Homo sapien calmodulin showing Ca+2' scene=''>
<StructureSection load='2bcx' size='340' side='right' caption='Homo sapien calmodulin showing Ca+2' scene=''>
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'''Calcium is an essential mineral that is needed in the human diet for proper functioning of neurons to strong bones and can also act as a second messenger for enzymes and proteins. Calmodulin (CaM), short for calcium modulated protein, is a small calcium binding protein with a three dimensional structure. Calmodulin has been known to be involved in various Ca2+ - dependent signal transduction pathways, can act as a Ca2+ sensor, and has been involved with regulated protein-kinases. 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
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Calcium is an essential mineral that is needed in the human diet for proper functioning of neurons to strong bones and can also act as a second messenger for enzymes and proteins. Calmodulin (CaM), short for calcium modulated protein, is a small calcium binding protein with a three dimensional structure. Calmodulin has been known to be involved in various Ca2+ - dependent signal transduction pathways, can act as a Ca2+ sensor, and has been involved with regulated protein-kinases. 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
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

Revision as of 00:15, 16 November 2015

Calmodulin

Homo sapien calmodulin showing Ca+2

Drag the structure with the mouse to rotate

References

1. Berridge, M. J., Lipp, P., & Bootman, M. D. (2000). The versatility and universality of calcium signalling. Nature Reviews Molecular Cell Biology, 1(1), 11-21. doi:10.1038/35036035

2. Eldik, L., & Watterson, D. (1998). Calmodulin and signal transduction. San Diego: Academic Press.

3. Huang, X., Liu, Y., Wang, R., Zhong, X., Liu, Y., Koop, A., Liu, Z. (2013). Two potential calmodulin-binding sequences in the ryanodine receptor contribute to a mobile, intra-subunit calmodulin-binding domain. Journal of Cell Science, 126(19), 4527–4535.

4. Joseph, J. D., & Means, A. R. (2002). Calcium Binding Is Required for Calmodulin Function in Aspergillus nidulans. Eukaryotic Cell, 1(1), 119–125. http://doi.org/10.1128/EC.01.1.119-125.2002

5. Lai, M., Brun, D., Edelstein, S. J., & Novere, N. L. (2015). Modulation of Calmodulin lobes by different targets: An allosteric model with hemi concerted conformational transitions. PLOS Computational Biology. http://doi:10.1371/journal.pcbi.1004063

6. Lukas, T. J., Haiech, J., Lau, W., Craig, T. A., Zimmer, W. E., Shattuck, R. L., et al. (1988). Calmodulin and calmodulin-regulated protein kinases as transducers of intracellular calcium signals. Cold Spring Harbor Symposia on Quantitative Biology, 53 Pt 1, 185-193.

7. Neri, D., de Lalla, C., Petrul, H., Neri, P., & Winter, G. (1995). Calmodulin as a versatile tag for antibody fragments. BioTechnology, 13, pp. 373–377

8. Wriggers, W., Mehler, E., Pitici, F., Weinstein, H., & Schulten, K. (1998). Structure and dynamics of Calmodulin in solution. Biophysical Journal, 74, 1622-1639.

9. Wolfe, D. M. D. M. (2006). Channeling studies in yeast: Yeast as a model for channelopathies? Neuromolecular Medicine, 8(3), 279; 279-306; 306.


  1. Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
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