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Sandbox GGC12
From Proteopedia
(Difference between revisions)
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== Relevance == | == Relevance == | ||
| - | IL-6 is produced is produced by wide range of cells that include not just cells of the immune system. Its production is induced by immune response, but can be affected by various antigenic factors. IL-6 binds to the IL-6 receptor of cells, which is then binded to the stignal-transducing receptor glycoprotein, known as gp130. This allows for the many functions of IL-6 in cells. Facilitating the roles that IL-6 plays in inducing cell growth and differentiation, other cytokines, immunoglobins, and acute phase proteins. | + | IL-6 is produced is produced by wide range of cells that include not just cells of the immune system. Its production is induced by immune response, but can be affected by various antigenic factors. IL-6 binds to the IL-6 receptor of cells, which is then binded to the stignal-transducing receptor glycoprotein, known as gp130. This allows for the many functions of IL-6 in cells. Facilitating the roles that IL-6 plays in inducing cell growth and differentiation, other cytokines, immunoglobins, and acute phase proteins. IL-6-mediated signal transduction is made possible by clustering of two gp130 receptors by IL-6. IL-6 binds to binds to a single molecule of IL-6r and forms a heterodimer. The heterodimer then binds to gp130 to form a heterotrimer. An additional binding step is then needed to achieve signal transduction through clustering.<ref>Somers, William. "1.9 A? crystal structure of interleukin 6: implications for a novel mode of receptor dimerization and signaling." The EMBO Journal.</ref> |
In the case of Castleman Disease, researchers have been working IL-6 with the goal that blocking the functions of IL-6 will alleviate the symptoms of afflicted patients. IL-6 blocking can be achieved through a variety of methods such as: inhibiting IL-6 production, IL-6 binding on IL-6 receptor, and interrupting intracellular signaling.<ref>Yoshizaki, Kazuyuki. "The Role of Interleukin-6 in Castleman Disease." Hematol Oncol Clin N Am.</ref> | In the case of Castleman Disease, researchers have been working IL-6 with the goal that blocking the functions of IL-6 will alleviate the symptoms of afflicted patients. IL-6 blocking can be achieved through a variety of methods such as: inhibiting IL-6 production, IL-6 binding on IL-6 receptor, and interrupting intracellular signaling.<ref>Yoshizaki, Kazuyuki. "The Role of Interleukin-6 in Castleman Disease." Hematol Oncol Clin N Am.</ref> | ||
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. | ||
| - | The structure of IL-6 is composed of four helices: A, B, C, and D. Helices A and B run in opposite direction to helices C and D. Helix A is connected to B which is connected to C; then C is connected to D.<ref>Somers, William. "1.9 A? crystal structure of interleukin 6: implications for a novel mode of receptor dimerization and signaling." The EMBO Journal.</ref> | + | IL-6 is a 185 amino acid polypeptide. The structure of IL-6 is composed of four helices: A, B, C, and D. Helices A and B run in opposite direction to helices C and D. Helix A is connected to B which is connected to C; then C is connected to D. There is also an additional mini-helix.<ref>Somers, William. "1.9 A? crystal structure of interleukin 6: implications for a novel mode of receptor dimerization and signaling." The EMBO Journal.</ref> |
<scene name='78/781196/4_helices/1'> Here you are able to get a clear view of the four helices that form IL-6. </scene> | <scene name='78/781196/4_helices/1'> Here you are able to get a clear view of the four helices that form IL-6. </scene> | ||
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<scene name='78/781196/Helix_d/1'>Here you are able to get a clear view of Helix D.</scene> | <scene name='78/781196/Helix_d/1'>Here you are able to get a clear view of Helix D.</scene> | ||
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| + | <scene name='78/781196/Helix_e/1'>Here you are able to get a clear view of the mini-helix lying outside the main helices bundle.</scene> | ||
<scene name='78/781196/Disulfide_linkage_aandb/2'>Here you are able to get a clear view of the disulfide linkage between Helix A and Helix B. </scene> | <scene name='78/781196/Disulfide_linkage_aandb/2'>Here you are able to get a clear view of the disulfide linkage between Helix A and Helix B. </scene> | ||
Revision as of 13:16, 23 April 2018
Structure: Human Interleukin-6
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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
- ↑ Somers, William. "1.9 A? crystal structure of interleukin 6: implications for a novel mode of receptor dimerization and signaling." The EMBO Journal.
- ↑ Somers, William. "1.9 A? crystal structure of interleukin 6: implications for a novel mode of receptor dimerization and signaling." The EMBO Journal.
- ↑ Yoshizaki, Kazuyuki. "The Role of Interleukin-6 in Castleman Disease." Hematol Oncol Clin N Am.
- ↑ Somers, William. "1.9 A? crystal structure of interleukin 6: implications for a novel mode of receptor dimerization and signaling." The EMBO Journal.
- ↑ Yoshizaki, Kazuyuki. "The Role of Interleukin-6 in Castleman Disease." Hematol Oncol Clin N Am.
- ↑ Somers, William. "1.9 A? crystal structure of interleukin 6: implications for a novel mode of receptor dimerization and signaling." The EMBO Journal.
- ↑ Somers, William. "1.9 A? crystal structure of interleukin 6: implications for a novel mode of receptor dimerization and signaling." The EMBO Journal.
- ↑ Somers, William. "1.9 A? crystal structure of interleukin 6: implications for a novel mode of receptor dimerization and signaling." The EMBO Journal.
