Sandbox Reserved 1227
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==MDM2== | ==MDM2== | ||
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== Function == | == Function == | ||
| - | MDM2 is a E3 ubiquitin ligase that is specific to the p53 pathway. MDM2 is one of the main negatively regulatory proteins of the p53 pathway. Often, the p53 pathway is compromised due to the inactivation of MDM2 which is thought to be one of the lead causes of tumor progression. It is believed that further MDM2 research and therapy could possibly lead to an anticancer strategy | + | MDM2 is a E3 ubiquitin ligase that is specific to the p53 pathway. MDM2 is one of the main negatively regulatory proteins of the p53 pathway. Often, the p53 pathway is compromised due to the inactivation of MDM2 which is thought to be one of the lead causes of tumor progression. It is believed that further MDM2 research and therapy could possibly lead to an anticancer strategy <ref>Trino, S., De Luca, L., Laurenzana, I., Caivano, A., Del Vecchio, L., Martinelli, G., & Musto, P. (2016). P53-MDM2 Pathway: Evidences for A New Targeted Therapeutic Approach in B-Acute Lymphoblastic Leukemia. Frontiers in Pharmacology, 7, 491. http://doi.org/10.3389/fphar.2016.00491.</ref>. Although there is a lot of research currently underway that involves the MDM2-p53 interactions, it is unsure exactly how these two molecules react. This is because part of MDM2’s receptor structure contains highly flexible parts. There is evidence that has shown that as the binding with p53 occurs, the MDM2 structure changes conformation from “closed” to “open.” In the closed conformation, there is an N-terminus fragment (residues 25-109) that forms a lid that covers its hydrophobic binding site. This shows that there are many intermediate levels of binding for the MDM2 complex. During the interaction with p53, it is thought that the N-terminus fragment interacts with a short, helical region of p53 <ref>Ciemny, M. P., Debinski, A., Paczkowska, M., Kolinski, A., Kurcinski, M., & Kmiecik, S. (2016). Protein-peptide molecular docking with large-scale conformational changes: the p53-MDM2 interaction. Scientific Reports, 6, 37532. http://doi.org/10.1038/srep37532.</ref>. |
== Disease == | == Disease == | ||
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</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
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Revision as of 20:51, 8 March 2017
| This Sandbox is Reserved from Jan 17 through June 31, 2017 for use in the course Biochemistry II taught by Jason Telford at the Maryville University, St. Louis, USA. This reservation includes Sandbox Reserved 1225 through Sandbox Reserved 1244. |
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MDM2
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References
- ↑ Trino, S., De Luca, L., Laurenzana, I., Caivano, A., Del Vecchio, L., Martinelli, G., & Musto, P. (2016). P53-MDM2 Pathway: Evidences for A New Targeted Therapeutic Approach in B-Acute Lymphoblastic Leukemia. Frontiers in Pharmacology, 7, 491. http://doi.org/10.3389/fphar.2016.00491.
- ↑ Ciemny, M. P., Debinski, A., Paczkowska, M., Kolinski, A., Kurcinski, M., & Kmiecik, S. (2016). Protein-peptide molecular docking with large-scale conformational changes: the p53-MDM2 interaction. Scientific Reports, 6, 37532. http://doi.org/10.1038/srep37532.
