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TitleCryo-EM structures reveal distinct apo conformations of sortilin-related receptor SORLA.
Journal, issue, pagesBiochem Biophys Res Commun, Vol. 600, Page 75-79, Year 2022
Publish dateApr 16, 2022
AuthorsXi Zhang / Cang Wu / Zhihong Song / Dayong Sun / Liting Zhai / Chuang Liu /
PubMed AbstractSorting-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 ...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.
External linksBiochem Biophys Res Commun / PubMed:35196630
MethodsEM (single particle)
Resolution3.4 Å
Structure data

32117

7vt0

EMDB-32117, PDB-7vt0:
Dimer structure of SORLA
Method: EM (single particle) / Resolution: 3.4 Å

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / Protein sorting receptor

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