User:Elizabeth G. Aylesworth/Sandbox 1
From Proteopedia
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acids and a coiled-coil structure. Unlike the long coronin, the short coronin’s N-terminal consists | acids and a coiled-coil structure. Unlike the long coronin, the short coronin’s N-terminal consists | ||
twelve amino acids(11). | twelve amino acids(11). | ||
+ | |||
As part of the WD40-repeat protein suprafamily, coronin are expected to have at least a | As part of the WD40-repeat protein suprafamily, coronin are expected to have at least a | ||
repeated sequence of four WDs as well as a propeller. When the structure was determined, it | repeated sequence of four WDs as well as a propeller. When the structure was determined, it | ||
- | was found that | + | was found that coronins have a repeated sequence of five, and instead of a five beta-propeller, |
it has a seven beta-propeller. | it has a seven beta-propeller. | ||
+ | |||
Three variants of coronin-1C have been identified in humans. This affects the region just before | Three variants of coronin-1C have been identified in humans. This affects the region just before | ||
the coiled-coil area of the coronin protein as well as the N-terminal being elongated compared to | the coiled-coil area of the coronin protein as well as the N-terminal being elongated compared to | ||
other coronin proteins. This protein, though complete structure has not been confirmed, does | other coronin proteins. This protein, though complete structure has not been confirmed, does | ||
have oligomeric properties(11). | have oligomeric properties(11). | ||
+ | |||
Dictyostelium discoideum was the first organism in which coronin was identified. Since that discovery in 1991, plants are the only eukaryotes that coronin has not been identified. There are 12 subfamilies, and half of them are found only in vertebrates (1. | Dictyostelium discoideum was the first organism in which coronin was identified. Since that discovery in 1991, plants are the only eukaryotes that coronin has not been identified. There are 12 subfamilies, and half of them are found only in vertebrates (1. | ||
== Function == | == Function == |
Current revision
Coronin
Coronin 1C
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References
- ↑ 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
- ↑ 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
1. Clemen C.S., Rybakin V., Eichinger L. (2008) The Coronin Family of Proteins. In: Clemen C.S., Eichinger L., Rybakin V. (eds) The Coronin Family of Proteins. Subcellular Biochemistry, vol 48. Springer, New York, NY.
2. Uniport. COR1C_MOUSE. 2019. https://www.uniprot.org/uniprot/Q9WUM4
3. Roadcap DW.; Clemen CS.; Bear, JE. Madame Curie Bioscience Database. The Role of Mammalian Coronins in Development and Disease. 2013. https://www.ncbi.nlm.nih.gov/books/NBK6528/
4. Meghal Gandhi and Bruce L Goode. Coronin: The Double-Edged Sword of Actin Dynamics. In: Madame Curie Bioscience Database [Internet]. Landes Bioscience; 2000-2013
5. McArdle B, Hofmann A. Coronin Structure and Implications. In: Madame Curie Bioscience Database [Internet]. Landes Bioscience; 2000-2013
6. Chan, K., Roadcap, D., Holoweckyj, N., Bear, J., Biochemical Journal. Coronin 1C harbours a second actin biding site that confers co-operative binding to F-Actin. 2012. 444. 89-96.
7. Long Wu, Chun-Wei Peng et. al. Journal of Experimental and Clinical Cancer Research; 29:17. BioMed Central, 24 February 2010.
8. Tokarz-Deptula, B.; Malinowska, M.; Adamiak, M.; Deptula, W. Coronins and their role in immunological phenomena. Central European Journal of Immunology 2017 DOI: 10.3897/bdj.4.e7720.figure2f.
9. Behrens J., Solga R., et all. Coronin 1C-free primary mouse fibroblasts exhibit robust rearrangements in the orientation of actin filamnets, microtublues and intermediate filaments. European Journal of Cell Biology. 2016. 8. 239-251.
10. Sokolova, O., Chemeris, A., Goode, B. Structural Basis of Arp 2/3 Complex Inhibition by GMF, Coronin, and Arpin. Journal of Molecular Biology. 2017. 237-248.
11. Christian Eckert, Bjorn Hammesfahr, and Martin Kollm. BMC Evol Biol. 2011; 11: 268.