dc.contributor.author |
Konstantakaki, M |
en |
dc.contributor.author |
Changeux, J |
en |
dc.contributor.author |
Taly, A |
en |
dc.date.accessioned |
2014-06-06T06:47:31Z |
|
dc.date.available |
2014-06-06T06:47:31Z |
|
dc.date.issued |
2007 |
en |
dc.identifier.uri |
http://dx.doi.org/10.1016/j.bbrc.2007.05.126 |
en |
dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/3647 |
|
dc.subject |
Acetylcholine |
en |
dc.subject |
Binding Protein |
en |
dc.subject |
Complex Structure |
en |
dc.subject |
Drug Design |
en |
dc.subject |
Nicotinic Acetylcholine Receptor |
en |
dc.subject |
Nicotinic Receptor |
en |
dc.subject |
protein-protein docking |
en |
dc.subject |
Resting State |
en |
dc.subject |
Rigid Body |
en |
dc.subject |
Long Chain |
en |
dc.title |
Docking of α-cobratoxin suggests a basal conformation of the nicotinic receptor |
en |
heal.type |
journalArticle |
en |
heal.identifier.primary |
10.1016/j.bbrc.2007.05.126 |
en |
heal.publicationDate |
2007 |
en |
heal.abstract |
We investigate the interactions between the long chain α-cobratoxin (Cbtx) and the nicotinic acetylcholine receptor using a rigid body docking procedure. The method, (i) reproduces the binding of Cbtx to Lymnea acetylcholine-binding protein (AChBP); (ii) shows that most of the structures of AChBP obtained in the presence of antagonists are compatible with Cbtx binding; and (iii) reveals a complex between |
en |
heal.journalName |
Biochemical and Biophysical Research Communications |
en |
dc.identifier.doi |
10.1016/j.bbrc.2007.05.126 |
en |