Sandbox Reserved 1110

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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.
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Contents

5LSD

5LSD is the recombinant mouse Nerve Growth Factor (NGF), that does not bind to any ligand. Therefore it allows conclusions on the features of its binding loops. Through 5LSD, 3 questions can be targeted: (i) how is the NGF N-terminus structured in the absence of ligands? (ii) how flexible/rigid are the loops and how does their dynamics may reflect on the overall structural plasticity of mature NGF? (iii) how much do the loops contribute to antibody recognition? [1]

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.

Structure

In the absence of Partners, the NGF N-terminus has a strong tendency to fold into a helix. This challenges the current view that this region is unstructured. [2]


References

  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. ↑ 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
[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

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