7VT0

Dimer structure of SORLA

Summary for 7VT0

• Entry DOI: 10.2210/pdb7vt0/pdb
• EMDB information: 32117
• Descriptor: Sortilin-related receptor (1 entity in total)
• Functional Keywords: protein sorting receptor, membrane protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 149671.78

Authors

Xi, Z.,Cang, W.,Chuang, L. (deposition date: 2021-10-27, release date: 2022-11-02, Last modification date: 2024-10-30)

Primary citation

Zhang, X.,Wu, C.,Song, Z.,Sun, D.,Zhai, L.,Liu, C.
Cryo-EM structures reveal distinct apo conformations of sortilin-related receptor SORLA.
Biochem.Biophys.Res.Commun., 600:75-79, 2022

PubMed Abstract: Sorting-related receptor with A-type repeats (SORLA) is an important receptor for regulating normal cellular functions via protein sorting. Here, we determined the structures of the full-length SORLA and identified two distinct conformations of apo-SORLA using single-particle cryogenic electron microscopy. In contrast to homologous proteins, both monomer and dimer forms of SORLA existed in a neutral solution. Only three hydrogen bonds in the vicinity of the dimer interface implied the involvement in dimerization. The orientation of residue R490 was a key point for ligand binding. These results suggest a unique mechanism of SORLA dimerization for protein trafficking.

PubMed: 35196630
DOI: 10.1016/j.bbrc.2022.01.108

Experimental method

ELECTRON MICROSCOPY (3.4 Å)