Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 600, Issue -, Pages 75-79Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2022.01.108
Keywords
Apo-SORLA; Cryo-EM structure; Conformation change; Dimerization
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Funding
- NSFC [31900868]
- Medical Scientific Research Foundation of Guangdong Province of China [A2021333]
- Shenzhen Peacock Program-Project Development Fund [20190904141C]
- Cryo-EM center of SUSTech
- Analysis and Testing Center of SUSTech
- Public Experiment Platform of SUSTech
- [JCYJ20200109141638004]
- [JCYJ20190808120613189]
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In this study, the structures of full-length SORLA were determined and two distinct conformations of apo-SORLA were identified using single-particle cryogenic electron microscopy. Unlike homologous proteins, SORLA existed in both monomer and dimer forms in a neutral solution. Only three hydrogen bonds near the dimer interface were involved in dimerization, and the orientation of residue R490 played a key role in ligand binding. These findings reveal a unique mechanism of SORLA dimerization for protein trafficking.
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. (c) 2022 Elsevier Inc. All rights reserved.
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