Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors
By Katjua Brejc, W. Dijk, R. Klaassen, M. Schuurmans, J. van der Oost, A. Smit, T. Sixma. Nature, 2001
1,755 citations recorded by the source corpus.
Subfields: Molecular Biology, Pharmacology
View Paper: https://www.semanticscholar.org/paper/62a76fb236b83c61d1151b1f8ebff41b045f3521
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Citations in the corpus
- GABAA Receptors: Subtypes Provide Diversity of Function and Pharmacology (2008, positive): “This has been combined with X-ray crystallography data on the homologous snail soluble acetylcholine binding protein (AChBP; Brejc et al., 2001), recently followed by that of the water soluble portion of the muscle nicotinic acetylcholine receptor (Dellisanti et al., 2007) and that of a related…”
- Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures. (2004, methodology): “Structure of theing the AChBP pentamer (Brejc et al., 2001) as search model.”
- Crystal structure of a Cbtx–AChBP complex reveals essential interactions between snake α‐neurotoxins and nicotinic receptors (2005, methodology): “In the complex, the loop C tip, comprised of residues Tyr185–Tyr192 and the Cys187–Cys188 disulfide bridge (Figure 1A), is markedly dislodged from its close apposition to the complementary face of the subunit interface seen in Hepes-bound AChBP (Brejc et al, 2001) (Figure 5).”
- Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations (2005, background): “This movement, which differs from the 3–41 movement of subunits observed between the Hepes- and PnIAbound AChBP structures (Celie et al, 2005), indicates that ligand binding may induce selective influences on the orientation of the subunits within the pentamer.”
- Molecular structure and function of the glycine receptor chloride channel. (2004, background): “The crystal structure of this protein (52) repre-”