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-Structure paper
タイトル | Cryo-EM structures reveal distinct apo conformations of sortilin-related receptor SORLA. |
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ジャーナル・号・ページ | Biochem Biophys Res Commun, Vol. 600, Page 75-79, Year 2022 |
掲載日 | 2022年4月16日 |
著者 | Xi Zhang / Cang Wu / Zhihong Song / Dayong Sun / Liting Zhai / Chuang Liu / |
PubMed 要旨 | 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 ...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. |
リンク | Biochem Biophys Res Commun / PubMed:35196630 |
手法 | EM (単粒子) |
解像度 | 3.4 Å |
構造データ | EMDB-32117, PDB-7vt0: |
由来 |
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キーワード | MEMBRANE PROTEIN / Protein sorting receptor |