| dc.contributor.author |
Konstantakaki, M |
en |
| dc.contributor.author |
Tzartos, SJ |
en |
| dc.contributor.author |
Poulas, K |
en |
| dc.contributor.author |
Eliopoulos, E |
en |
| dc.date.accessioned |
2014-06-06T06:48:51Z |
|
| dc.date.available |
2014-06-06T06:48:51Z |
|
| dc.date.issued |
2008 |
en |
| dc.identifier.issn |
10933263 |
en |
| dc.identifier.uri |
http://dx.doi.org/10.1016/j.jmgm.2008.01.004 |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/4297 |
|
| dc.subject |
α1 nAChR |
en |
| dc.subject |
α7 nAChR |
en |
| dc.subject |
Extracellular domain |
en |
| dc.subject |
Homology model |
en |
| dc.subject |
Ligand-binding domain |
en |
| dc.subject |
Rational drug design |
en |
| dc.subject |
Structure |
en |
| dc.subject.other |
Crystal structure |
en |
| dc.subject.other |
Disease control |
en |
| dc.subject.other |
Monomers |
en |
| dc.subject.other |
Three dimensional |
en |
| dc.subject.other |
Extracellular domain |
en |
| dc.subject.other |
Homology models |
en |
| dc.subject.other |
Ligand-binding domain |
en |
| dc.subject.other |
Rational drug design |
en |
| dc.subject.other |
Drug products |
en |
| dc.subject.other |
alpha bungarotoxin |
en |
| dc.subject.other |
homodimer |
en |
| dc.subject.other |
monomer |
en |
| dc.subject.other |
nicotinic receptor |
en |
| dc.subject.other |
receptor subunit |
en |
| dc.subject.other |
article |
en |
| dc.subject.other |
binding site |
en |
| dc.subject.other |
crystal structure |
en |
| dc.subject.other |
drug design |
en |
| dc.subject.other |
labeling index |
en |
| dc.subject.other |
ligand binding |
en |
| dc.subject.other |
mutagenesis |
en |
| dc.subject.other |
priority journal |
en |
| dc.subject.other |
protein domain |
en |
| dc.subject.other |
Amino Acid Sequence |
en |
| dc.subject.other |
Animals |
en |
| dc.subject.other |
Binding Sites |
en |
| dc.subject.other |
Crystallography, X-Ray |
en |
| dc.subject.other |
Dimerization |
en |
| dc.subject.other |
Drug Design |
en |
| dc.subject.other |
Humans |
en |
| dc.subject.other |
Ligands |
en |
| dc.subject.other |
Mice |
en |
| dc.subject.other |
Models, Molecular |
en |
| dc.subject.other |
Molecular Sequence Data |
en |
| dc.subject.other |
Protein Structure, Secondary |
en |
| dc.subject.other |
Protein Structure, Tertiary |
en |
| dc.subject.other |
Receptors, Nicotinic |
en |
| dc.subject.other |
Sequence Homology, Amino Acid |
en |
| dc.title |
Model of the extracellular domain of the human α7 nAChR based on the crystal structure of the mouse α1 nAChR extracellular domain |
en |
| heal.type |
journalArticle |
en |
| heal.identifier.primary |
10.1016/j.jmgm.2008.01.004 |
en |
| heal.publicationDate |
2008 |
en |
| heal.abstract |
Neuronal nicotinic acetylcholine receptors (nAChRs) are important therapeutic targets for various diseases, including Alzheimer's disease, Parkinson's disease, and schizophrenia, as well as for cessation of smoking. Based on the recently determined crystal structure of the extracellular domain (ECD) of the mouse nAChR α1 subunit complexed with α-bungarotoxin at 1.94 Å resolution, we have constructed three-dimensional models of the ECD of the monomer, homodimer, and homopentamer of the human α7 nAChR and investigated in detail the interface between the two α7 subunits. The docking of the agonist in the ligand-binding pocket of the human α7 dimer was also performed and found consistent with results from labeling and mutagenesis experiments. Since the nAChR ligand-binding site is a useful target for mutagenesis studies and the rational design of drugs against diseases, these models provide useful information for future work. © 2008 Elsevier Inc. All rights reserved. |
en |
| heal.journalName |
Journal of Molecular Graphics and Modelling |
en |
| dc.identifier.issue |
8 |
en |
| dc.identifier.volume |
26 |
en |
| dc.identifier.doi |
10.1016/j.jmgm.2008.01.004 |
en |
| dc.identifier.spage |
1333 |
en |
| dc.identifier.epage |
1337 |
en |