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© Structural Dynamics Of Macromolecules
The structure of a bacterial analog of the nicotinic receptor (one color per subunit) inserted into the cell membrane (grey and orange). A representation of the volume accessible to ions is shown in yellow.
Publication :

Discovering cryptic pocket opening and binding of a stimulant derivative in a vestibular site of the 5-HT3A receptor

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in - 14 Nov 2024

Nandan Haloi, Emelia Karlsson, Marc Delarue, Rebecca J Howard, Erik Lindahl

Link to HAL – pasteur-04769582

Link to DOI – 10.1101/2023.11.13.566806

2024

Ligand-gated ion channels propagate electrochemical signals in the nervous system. A diverse set of allosteric modulators including stimulants, anesthetics, and lipids regulate their function; however, structures of ligand-bound complexes can be difficult to capture by experimental methods, particularly when binding is dynamic or transient. Here, we used computational methods and electrophysiology to identify a possible bound state of a modulatory stimulant derivative in a cryptic vestibular pocket of a mammalian serotonin-3A receptor. Starting from a closed-pocket experimental structure, we first applied a molecular dynamics simulations-based goal-oriented adaptive sampling method to identify possible open-pocket conformations. To find plausible ligand-binding poses, we performed Boltzmann docking, which combines traditional docking with Markov state modeling, of the newly sampled conformations. Clustering and analysis of stability and accessibility of docked poses supported a preferred binding site; we further 1.