Molecular docking of four [beta]-amyloid1-42 fragments on the [alpha]7 nicotinic receptor: delineating the binding site of the A[beta] peptides

@article{citeulike:2683157, abstract = {Three-dimensional structures of the complexes between the A[beta]1-42 fragments A[beta]1-11, A[beta]10-20, A[beta]12-28, and A[beta]22-35 and the [alpha]7 nicotinic receptor were obtained with the aid of the ESCHER program. Furthermore, short high-temperature molecular dynamics simulations in vacuo were employed to relax the complexes and allow the peptides to accommodate in the binding site. The final models have shown that A[beta] peptides do bind on the same site, which is delineated by loop C of one subunit and the loops 62-74 and G of the adjacent subunit on the receptor. This finding is supported by previous experimental and theoretical data, and should help one to obtain a better and more detailed structural information about the activity of the A[beta] peptides and their repercussion in the disorders at molecular level, which are characteristic of the Alzheimer's disease.}, author = {Espinoza-Fonseca, Michel L. }, citeulike-article-id = {2683157}, doi = {10.1016/j.bbrc.2004.08.218}, journal = {Biochemical and Biophysical Research Communications}, keywords = {ion\_channels, pdb2pqr, protein-protein\_interactions}, month = {October}, number = {4}, pages = {1191--1196}, posted-at = {2008-04-17 19:46:51}, priority = {0}, title = {Molecular docking of four [beta]-amyloid1-42 fragments on the [alpha]7 nicotinic receptor: delineating the binding site of the A[beta] peptides}, url = {http://dx.doi.org/10.1016/j.bbrc.2004.08.218}, volume = {323}, year = {2004} }

TY - JOUR ID - citeulike:2683157 L3 - citeulike-article-id:2683157 TI - Molecular docking of four [beta]-amyloid1-42 fragments on the [alpha]7 nicotinic receptor: delineating the binding site of the A[beta] peptides JF - Biochemical and Biophysical Research Communications VL - 323 IS - 4 SP - 1191 EP - 1196 N2 - Three-dimensional structures of the complexes between the A[beta]1-42 fragments A[beta]1-11, A[beta]10-20, A[beta]12-28, and A[beta]22-35 and the [alpha]7 nicotinic receptor were obtained with the aid of the ESCHER program. Furthermore, short high-temperature molecular dynamics simulations in vacuo were employed to relax the complexes and allow the peptides to accommodate in the binding site. The final models have shown that A[beta] peptides do bind on the same site, which is delineated by loop C of one subunit and the loops 62-74 and G of the adjacent subunit on the receptor. This finding is supported by previous experimental and theoretical data, and should help one to obtain a better and more detailed structural information about the activity of the A[beta] peptides and their repercussion in the disorders at molecular level, which are characteristic of the Alzheimer's disease. KW - ion_channels KW - pdb2pqr KW - protein-protein_interactions AU - Espinoza-Fonseca, Michel PY - 2004/10/29/ UR - http://dx.doi.org/10.1016/j.bbrc.2004.08.218 ER -