User:Luke Houston/sandbox 1
From Proteopedia
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== Function == | == Function == | ||
| - | The protein chordin has many different functions that it serves inside of the embryos of various organisms. | + | The protein chordin has many different functions that it serves inside of the embryos of various organisms. Each function that it possesses allows for life to form and function normally within these different organisms. One of the important functions that chordin serves is monitoring and regulating the BMP of embryos. BMP stands for bone morphogenetic proteins. These are proteins that help an organism develop various organs and body parts. For the Xenopus, chordin blocks these BMP from sending signals to one another. What happens is that chordin will bind or attach itself onto a bone morphogenetic protein. By doing this, it blocks the BMP from sending signals to other BMP within the cells. The reason that this is an important function is that by chordin blocking the bone morphogenetic proteins, it prevents an epidermis from forming on the organism. Xenopus are not in need of having an epidermis, so preventing it from forming is very important in embryological development. Also by chordin blocking the bone morphogenetic proteins, the central nervous system can be differentiated. This differentiation allows for the secondary embryo of the organism to develop that proper way. Without this, an organism could develop poorly and cause problems once outside of the egg or mother. Chordin is very essential in this regard. Another function that we see for the protein chordin is that chordin is responsible for creating a gradient formation in the space between the ectoderm and the endomesoderm. Chordin, and the aforementioned BMP, are very involved and responsible for impacting the three germ layers. These are the ectoderm, mesoderm, and endoderm. These chordin proteins will also work together with the bone morphogenetic proteins to help provide the information for the patterning of the germ layers in the cell. This is why it is important for chordin to be with the BMP and within the extracellular space of the cell. Chordin has to be within this space because that is how it can find and bind to the BMP. Within chordin being within the extracellular space, a gradient of separation with the ectoderm and the endomesoderm. A space that is now known as a Brachet's Cleft. Essentially what Brachet's Cleft is a model to show and describe tissue separation. In this space, cells are able to read and work with the chordin, and BMP, to help build and create the cells and organisms to develop a correct embryo. These chordin and BMP matrix provide the information that allows for patterning for the germ layers of the cell. Chordin will also serve a very important function for the Spemann Organizer. This is an organizer within cells that will allow or induce the formation of dorsal tissues. It is also common that chordin will mutate and formless dorsal tissue within the zebrafish. |
== Disease == | == Disease == | ||
| + | With the chordin protein, some diseases can be associated with it. One disorder that has been linked to the chordin protein is named cornelia de lange syndrome. This disease is when there are problems with the growth of an organism. This includes being too small or too big but also affecting the different sizes of structures that are within the body as well. These effects can happen before birth, so during embryo development, or after birth. Typically with chordin, the problem is seen while the organism is still considered an embryo. Another related disease is known as holoprosencephaly. This is a disease that is described a single-lobed brain with defects of facial features. | ||
== Relevance == | == Relevance == | ||
Chordin is a very relevant and considerable component for understanding and researching the ways that various embryos develop from the time that they are conceived to birth. It can also be considered relevant in what organisms do with the protein and how they can affect their lives after development. | Chordin is a very relevant and considerable component for understanding and researching the ways that various embryos develop from the time that they are conceived to birth. It can also be considered relevant in what organisms do with the protein and how they can affect their lives after development. | ||
== Structural highlights == | == Structural highlights == | ||
| - | + | The structure that is shown is a chordin protein that is model number 3B3K. This molecule is one that belongs to chordin family, but it is also a part of the BMP modulator protein. As discovered, bone morphogenetic proteins are very closely and associated with the chordin. This is why the structure is able to represent what a chordin protein might look like. This structure is known to work just like chordin protein would. It binds and attaches itself to a BMP to suppress or enhance the signal that it will be able to put out. This particular structure is made of three hundred and forty-two amino acids in its sequence. With this particular sequence, two mutations were also observed. The first mutation can be seen around amino acid forty. The second mutation is right around the ninety amino acid number. This particular chordin molecule was present inside of the zebrafish that was aforementioned earlier on this page. Interesting enough, this is a structure that is also closely linked to a protein that is present inside of homo sapiens. Within the structure, we are also able to see where in particular the bone morphogenetic structures are being suppressed or enhanced. Knowing and understanding the structure allows for a deeper understanding of the protein. | |
| - | This is a | + | |
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
| + | Anderson, R., Lawrence, A., Stottmann, R., Bachiller, D., & Klingensmith, J. (2002, November 01). Chordin and Noggin promote organizing centers of forebrain development in the mouse. Retrieved March 28, 2021, from https://dev.biologists.org/content/129/21/4975 | ||
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| + | B. (n.d.). Chordin. Retrieved March 28, 2021, from https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/chordin | ||
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| + | E. (n.d.). The chordin page. Retrieved March 28, 2021, from https://www.hhmi.ucla.edu/derobertis/EDR_MS/chd_page/chordin.html | ||
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| + | Edward M. DE ROBERTIS. (n.d.). Retrieved March 28, 2021, from https://www.biolchem.ucla.edu/people/edward-m-de-robertis/ | ||
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| + | Plouhinec, J., Zakin, L., Moriyama, Y., & Robertis, E. (2013, December 17). Chordin forms a Self-organizing morphogen gradient in the extracellular space between Ectoderm and mesoderm in The Xenopus Embryo. Retrieved March 28, 2021, from https://www.pnas.org/content/110/51/20372 | ||
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| + | M, S. B. D. M., M, B. L. Y. M., M, N. L. M., M, K. P. M., RS, B. G. U. K., M, K. A. A. M., … Z, R. J. A. (n.d.). Holoprosencephaly. MalaCards. https://www.malacards.org/card/holoprosencephaly. | ||
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| + | L, S. A. L., RC, K. A. D. H., RC, H. S. H., JK, G. J. H. B., J, G.-R. M. C. P., JR, Y. B. L., … A, R. E. M. (n.d.). Cornelia De Lange Syndrome. MalaCards. https://www.malacards.org/card/cornelia_de_lange_syndrome. | ||
<references/> | <references/> | ||
Current revision
Chordin
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References
Anderson, R., Lawrence, A., Stottmann, R., Bachiller, D., & Klingensmith, J. (2002, November 01). Chordin and Noggin promote organizing centers of forebrain development in the mouse. Retrieved March 28, 2021, from https://dev.biologists.org/content/129/21/4975
B. (n.d.). Chordin. Retrieved March 28, 2021, from https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/chordin
E. (n.d.). The chordin page. Retrieved March 28, 2021, from https://www.hhmi.ucla.edu/derobertis/EDR_MS/chd_page/chordin.html
Edward M. DE ROBERTIS. (n.d.). Retrieved March 28, 2021, from https://www.biolchem.ucla.edu/people/edward-m-de-robertis/
Plouhinec, J., Zakin, L., Moriyama, Y., & Robertis, E. (2013, December 17). Chordin forms a Self-organizing morphogen gradient in the extracellular space between Ectoderm and mesoderm in The Xenopus Embryo. Retrieved March 28, 2021, from https://www.pnas.org/content/110/51/20372
M, S. B. D. M., M, B. L. Y. M., M, N. L. M., M, K. P. M., RS, B. G. U. K., M, K. A. A. M., … Z, R. J. A. (n.d.). Holoprosencephaly. MalaCards. https://www.malacards.org/card/holoprosencephaly.
L, S. A. L., RC, K. A. D. H., RC, H. S. H., JK, G. J. H. B., J, G.-R. M. C. P., JR, Y. B. L., … A, R. E. M. (n.d.). Cornelia De Lange Syndrome. MalaCards. https://www.malacards.org/card/cornelia_de_lange_syndrome.
- ↑ 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
