Crystal structure of a Cbtx–AChBP complex reveals essential interactions between snake α‐neurotoxins and nicotinic receptors

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Towards automated crystallographic structure refinement with phenix.refine (2012, neutral): “Low-resolution structures The structures with PDB entries 1jl4 (Wang et al., 2001), 2gsz (Satyshur et al., 2007), 1yi5 (Bourne et al., 2005), 2wjx (Clayton et al., 2009), 3eob (Li et al., 2009), 1av1 (Brouillette & Anantharamaiah, 1995), 3bbw (Qiu et al., 2008) and 2i07 (Janssen et al., 2006) were…”
Molecular dynamics simulations and drug discovery (2011, background): “[12] proposed that the unbound AChBP and AChR are highly dynamic proteins that, in the absence of a ligand, sample many conformational states, both open and closed, that are selectively stabilized by the binding of agonists and antagonists.”
Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations (2005, background): “…a similar intermediate conformation as seen in the apo structure and the MLA–AAChBP complex, but it is tangentially displaced by B4 Å toward loop b7–b8 (Bourne et al, 2005), suggesting either a common mechanism for peptide toxin antagonism or that the Cbtx fingers lock loop C in a unique position.”
Mammalian Nicotinic Acetylcholine Receptors: From Structure to Function (2009, background): “This in effect caps the ligand binding site to trap the ligand deep inside as seen in Figure 2A (65, 171, 205).”