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On March 10, 2022, the team of researchers Sun Ziyi and Zhou Xiaoming of the State Key Laboratory of Biotherapy/Rare Disease Center/Department of Integrative Medicine, West China Hospital, Sichuan University published online in Nature Communications entitled "An open-like conformation of the sigma -1 receptor reveals its ligand entry pathway", which revealed the molecular mechanism of ligand entry into sigma-1 receptor through PATH2 pathway
Dr.
Sigma-1 receptor (σ1R) is a class of non-opioid transmembrane protein receptors, mainly located in the endoplasmic reticulum membrane of cells, distributed in most organs and tissues of the human body, and mediates cell survival and various physiological activities.
Figure 1.
This study used X-ray crystallography to resolve for the first time the openness of Xenopus laevis σ1R (xlσ1R) to bind endogenous ligands (presumed) and exogenous ligands (agonist PRE-084, antagonist S1RA), respectively / Closed high precision 3D structure
Figure 2.
On the other hand, the α4 helix in the open structure of xlσ1R undergoes rotational displacement, and the tyrosine side chain at position 203 on the α5 helix rotates inward, forming an opening that allows the passage of ligands (Fig.
Figure 3.
In conclusion, this study resolves the open structure of Xenopus laevis σ1R by X-ray crystallography, which supports the entry of σ1R ligands into the receptor β-barrel through the opening between the α4 and α5 helices (PATH2 pathway).
Original link: https://doi.