Cryo-EM structure studies of the human VPS10 domain-containing receptor SorCS3

Autor:	Fengquan Dong, Cang Wu, Weipeng Jiang, Maocai Zhai, Haiying Li, Liting Zhai, Xi Zhang
Rok vydání:	2022
Předmět:	Protein Transport Cryoelectron Microscopy Biophysics Humans Nerve Tissue Proteins Receptors Cell Surface Cell Biology Carrier Proteins Molecular Biology Biochemistry Protein Binding
Zdroj:	Biochemical and Biophysical Research Communications. 624:89-94
ISSN:	0006-291X
Popis:	The human VPS10 domain-containing receptor SorCS3 belongs to the Vps10p-domain receptor family and is an important receptor for regulating normal cellular functions via protein sorting. Here, we determined the cryo-EM structure of the full-length SorCS3 receptor and further found that there were at least three distinct conformations (monomer, M-shaped dimer and N-shaped dimer) of SorCS3 in the apo state. The differences between the two dimer conformations were caused by PKD1-2 assembly. In contrast to its homologous proteins, the conserved residues GLN198, ARG678, TYR430, GLU1020 and ASP1024 may be key points for its dimerization and for protein/polypeptide binding. These results showed the structural details of apo-SorCS3, which provides a foundation for elucidating the mechanism of protein sorting.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f03632d2af3d5b6378e0a7e18f77f926 https://doi.org/10.1016/j.bbrc.2022.07.009 Zobrazit plný text záznamu Full Text from ScienceDirect