Title : A computational investigation on the role of glycosylation in the binding of alpha1 nicotinic acetylcholine receptor with two alpha-neurotoxins.

Pub. Date : 2011 Jan

PMID : 21058296






2 Functional Relationships(s)
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1 Based on the crystal structure of the extracellular domain (ECD) of the mouse nicotinic acetylcholine receptor (nAChR) alpha1 subunit bound to alpha-bungarotoxin (alpha-Btx) we have generated in silico models of the human nAChR alpha1 bound to alpha-Btx and alpha-cobratoxin (alpha-Cbtx), both in the presence and in the absence of the N-linked carbohydrate chain. Nitrogen cholinergic receptor, nicotinic, alpha polypeptide 7 Mus musculus
2 Based on the crystal structure of the extracellular domain (ECD) of the mouse nicotinic acetylcholine receptor (nAChR) alpha1 subunit bound to alpha-bungarotoxin (alpha-Btx) we have generated in silico models of the human nAChR alpha1 bound to alpha-Btx and alpha-cobratoxin (alpha-Cbtx), both in the presence and in the absence of the N-linked carbohydrate chain. Nitrogen cholinergic receptor, nicotinic, alpha polypeptide 7 Mus musculus