Literature DB >> 15178425

Insights from modelling the 3D structure of the extracellular domain of alpha7 nicotinic acetylcholine receptor.

Kuo-Chen Chou1.   

Abstract

Based on the crystal structure of acetylcholine-binding protein, the three-dimensional structures of the extracellular domain, or the ligand-binding domains, of the monomer, homodimer, and homopentamer of the alpha7 nicotinic acetylcholine receptor were derived. The interface between two subunits, where the ligand-binding site is located, was investigated. Furthermore, an explicit definition of the ligand-binding pocket was illustrated that might provide useful clues for conducting various mutagenesis studies for finding drugs against schizophrenia and Alzheimer's disease.

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Year:  2004        PMID: 15178425     DOI: 10.1016/j.bbrc.2004.05.016

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  18 in total

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8.  Prediction of protein domain with mRMR feature selection and analysis.

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9.  Design novel dual agonists for treating type-2 diabetes by targeting peroxisome proliferator-activated receptors with core hopping approach.

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10.  Find novel dual-agonist drugs for treating type 2 diabetes by means of cheminformatics.

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