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Dynamics and Interactions of GPI-Linked Lynx1 Protein with/without Nicotinic Acetylcholine Receptor in Membrane Bilayers.

Nicotinic acetylcholine receptor (nAChR) participates in diverse biological processes, e.g., mood, learning, and addiction. Glycosylphosphatidylinositol (GPI)-linked lynx1 is an allosteric modulator of nAChR function, including shifts in agonist sensitivity, reduced desensitization, and slower recovery from desensitization. This modulation is thought to be achieved by lynx1's interaction with nAChR subunits, particularly at the α4:α4 interface. In this study, we used molecular modeling and simulation to study the structure, dynamics, and interactions of lynx1 when bound to nAChRs, as well as unbound, monomeric lynx1, when embedded in membranes. Though lynx1 structures are similar in both states, lynx1 dynamics are more restricted in the bound state than in the unbound one. When bound, interactions between lynx1 and nAChR are observed to be maintained throughout the simulations. Of particular note, lynx1 demonstrates prolonged interactions with the receptor C-loop in one of the nAChR α4 subunits, a region important for agonist binding and possibly the transition between open/close states. During interactions with lynx1, an α4 C-loop tends to be restricted in either close or open state, whereas the C-loop state transitions are more evident in when the nAChR is unbound by lynx1. Interestingly, the conformational change of the C-loop is stochastic, suggesting that lynx1 can influence nAChR (critical for its multimodal action), for instance by shifting its agonist sensitivity and recovery from desensitization.