7vt0

From Proteopedia

Dimer structure of SORLA

Structural highlights

7vt0 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.4Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SORL_HUMAN Likely to be a multifunctional endocytic receptor, that may be implicated in the uptake of lipoproteins and of proteases. Binds LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. Binds the receptor-associated protein (RAP). Could play a role in cell-cell interaction.

Publication Abstract from PubMed

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.

Cryo-EM structures reveal distinct apo conformations of sortilin-related receptor SORLA.,Zhang X, Wu C, Song Z, Sun D, Zhai L, Liu C Biochem Biophys Res Commun. 2022 Apr 16;600:75-79. doi: , 10.1016/j.bbrc.2022.01.108. Epub 2022 Feb 12. PMID:35196630^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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. 2022 Apr 16;600:75-79. PMID:35196630 doi:10.1016/j.bbrc.2022.01.108