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The Sigma-1 Receptor (S1R) is a small, ligand-regulated integral membrane protein involved in cell homeostasis and the cellular stress response. The receptor has a multitude of protein and small molecule interaction partners with therapeutic potential. Newly reported structures of the human S1R in ligand-bound states provides essential insights into small molecule binding in the context of the overall protein structure. The structure also raises many interesting questions and provides an excellent starting point for understanding the molecular tricks employed by this small membrane receptor to modulate a large number of signaling events. Here, we review insights from the structures of ligand-bound S1R in the context of previous biochemical studies and propose, from a structural viewpoint, a set of important future directions.

Original publication

DOI

10.1007/978-3-319-50174-1_3

Type

Journal article

Journal

Adv Exp Med Biol

Publication Date

2017

Volume

964

Pages

15 - 29

Keywords

Ligand binding, Membrane protein, Protein oligomerization, Protein structure, Sigma-1 receptor, Amino Acid Sequence, Animals, Humans, Ligands, Receptors, sigma, Sequence Alignment, Small Molecule Libraries