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	== Function ==		== Function ==
-	CAL1_HOMO	+	(Find functions of calmodulin) Calmodulin's target proteins come in various shapes, sizes and sequences and are involved in a wide array of functions. For example, calcium-bound calmodulin forms a critical subunit for the regulatory enzyme phosphorylase kinase, which in turn is a regulator for glycogen breakdown. Calmodulin also binds and activates other kinases and phosphatases that play significant roles in cell signaling, ion transport and cell death. One common theme in the contact between calmodulin and its different target proteins is the use of non-polar interactions, in particular, through the interactions with the unusually abundant methionines of calmodulin. Calcium binding exposes these non-polar surfaces of calmodulin, which then bind to non-polar regions on the target proteins.
-	== Disease ==	+	== NMR Structure ==
-	dystrophy	+	NMR studies clearly show that the connector between the two calcium binding globular domains is flexible even when it is not bound to its target proteins. However, the full range of flexibility can be seen in calmodulin's interactions with its target proteins. Calmodulin typically wraps around its target, with the two globular domains gripping either side of it.
	== Relevance ==		== Relevance ==
	common		common

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Revision as of 23:28, 14 November 2015

Calmodulin

spinqualitylabelsall models Homo sapien calmodulin showing Ca+2 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Calmodulin (CaM), short for calcium modulated protein, is a small calcium binding protein with a three dimensional structure. It has a molecular mass of 16 kilodaltons (kD) and it functions along with ryanodine receptor (RyR). You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue. Contents 1 Function 2 NMR Structure 3 Relevance 4 Structural highlights Function (Find functions of calmodulin) Calmodulin's target proteins come in various shapes, sizes and sequences and are involved in a wide array of functions. For example, calcium-bound calmodulin forms a critical subunit for the regulatory enzyme phosphorylase kinase, which in turn is a regulator for glycogen breakdown. Calmodulin also binds and activates other kinases and phosphatases that play significant roles in cell signaling, ion transport and cell death. One common theme in the contact between calmodulin and its different target proteins is the use of non-polar interactions, in particular, through the interactions with the unusually abundant methionines of calmodulin. Calcium binding exposes these non-polar surfaces of calmodulin, which then bind to non-polar regions on the target proteins. NMR Structure NMR studies clearly show that the connector between the two calcium binding globular domains is flexible even when it is not bound to its target proteins. However, the full range of flexibility can be seen in calmodulin's interactions with its target proteins. Calmodulin typically wraps around its target, with the two globular domains gripping either side of it. Relevance common Structural highlights secondary structure This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

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