Sandbox Reserved 1110

From Proteopedia

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This Sandbox is Reserved from 25/11/2019, through 30/9/2020 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1091 through Sandbox Reserved 1115.

To get started: Click the edit this page tab at the top. Save the page after each step, then edit it again. show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page. Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc. More help: Help:Editing

5LSD: A recombinant version of NGF

spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs. 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 The neurotrophin family 2 Disease and use in Biotechnologies 3 Relevance link title 4 Differences and importance of unbounded feature The neurotrophin family Disease and use in Biotechnologies Relevance link title As NGF is the prototype of the neurotrophin family, a better understanding of NGF could lead to a better understanding of the whole family. Knowledge of 5LSD could support this. Differences and importance of unbounded feature 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. ↑ 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

[1]Paoletti F, de Chiara C, Kelly G, Covaceuszach S, Malerba F, Yan R, Lamba D, Cattaneo A, Pastore A. Conformational Rigidity within Plasticity Promotes Differential Target Recognition of Nerve Growth Factor. Front Mol Biosci. 2016 Dec 26;3:83. doi: 10.3389/fmolb.2016.00083. eCollection, 2016. PMID:28083536 doi:http://dx.doi.org/10.3389/fmolb.2016.00083.

[2]Tiveron C1, Fasulo L, Capsoni S, Malerba F, Marinelli S, Paoletti F, Piccinin S, Scardigli R, Amato G, Brandi R, Capelli P, D'Aguanno S, Florenzano F, La Regina F, Lecci A, Manca A, Meli G, Pistillo L, Berretta N, Nisticò R, Pavone F, Cattaneo A. ProNGF\NGF imbalance triggers learning and memory deficits, neurodegeneration and spontaneous epileptic-like discharges in transgenic mice. Cell Death Differ. 2013 Aug;20(8):1017-30. doi: 10.1038/cdd.2013.22. [3] B. A. Mysona, S. Matragoon, M. Stephens, I. N. Mohamed, A. Farooq, M. L. Bartasis, A. Y. Fouda, A. Y. Shanab, D. G. Espinosa-Heidmann, 2 and A. B. El-Remessy Imbalance of the Nerve Growth Factor and Its Precursor as a Potential Biomarker for Diabetic Retinopathy. Biomed Res Int. 2015; 2015: 571456. doi: 10.1155/2015/571456. [4] McDonald NQ, Lapatto R, Murray-Rust J, Gunning J, Wlodawer A, Blundell TL. New protein fold revealed by a 2.3-A resolution crystal structure of nerve growth factor. Nature. 1991 Dec 5;354(6352):411-4. doi: 10.1038/354411a0. [5]M. Pattarawarapan and K. Burgess (2003) Molecular basis of Neurotrophin-Receptor Interactions. Journal of Medicinal Chemistry 46, 5277-5291. [6] M. Bibel and Y.-A. Barde (2000) Neurotrophins: Key Regulators of Cell Fate and Cell Shape in the Vertebrate Nervous System. Genes and Development 14, 2919-2937