crystallization-proteins-on-chip-microdialysis-for-situ-x-ray

Crystallization of Proteins on Chip by Microdialysis for <i>In Situ</i> X-ray Diffraction Studies

This protocol describes the manufacturing of reproducible and inexpensive microfluidic devices covering the whole pipeline for crystallizing proteins ...

Université Grenoble Alpes, CEA, CNRS, IBS

Crystal structure of the ligand-binding domain of the retinoid X receptor from the ascidian Polyandrocarpa misakiensis.

Alzheimer's disease is a growing concern in the context of the increasing lifespan of the populations. The work presented here is part of the fight against this threat. It supports a therapeutic approach to reduce the incidence of Alzheimer's disease, taking advantage of the specific binding of several domains of Netrin-1 to the β-amyloid precursor protein. This basic knowledge shall then be used to predict, design or characterize lead compounds that may in turn inhibit/delay Alzheimer's disease's progression, extending the therapeutic offer of the other leads already being investigated in this line. The present work is focused on the interaction of the various portions of APP with the three domains of Netrin-1, the so-called LamNT, EGF-like and NTR domains respectively. It reveals in detail which portions of APP and Netrin-1 are specifically involved in these interactions, using ELISA technique in combination with protein-protein binding simulations. So far unsuspected interaction sites located in Netrin-1 EGF-like and NTR domains open possibilities for new therapeutic approaches in which these sites will be specifically targeted.

Article	Year
Crystal structure of the ligand-binding domain of the retinoid X receptor from the ascidian Polyandrocarpa misakiensis. Proteins\| PubMed ID: 19004016	2009
Molecular characterization of Netrin-1 and APP receptor binding: New leads to block the progression of senile plaques in Alzheimer's disease. Biochemical and biophysical research communications\| PubMed ID: 28501620	2017

Franck Borel

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