9JUQ
Cryo-EM structure of transporter2a1
9JUQ の概要
| エントリーDOI | 10.2210/pdb9juq/pdb |
| EMDBエントリー | 61834 |
| 分子名称 | Solute carrier organic anion transporter family member 2A1 (1 entity in total) |
| 機能のキーワード | mfs family transporter, transport protein |
| 由来する生物種 | Homo sapiens (human) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 70103.90 |
| 構造登録者 | |
| 主引用文献 | Xia, Z.,Lu, G.,Wu, D.,Zhao, J.,Zhang, B.,Xu, H.,Du, Y.,Jiang, D. Structure and transport mechanism of the human prostaglandin transporter SLCO2A1. Nat Commun, 16:8124-8124, 2025 Cited by PubMed Abstract: SLCO2A1 is a member of the organic anion transporting polypeptide (OATP) family, which preferentially transports prostaglandins (PGs) into cells and plays a vital role in regulating PGs inactivation and distribution. Dysregulation or genetic mutation of SLCO2A1 is associated with primary hypertrophic osteoarthropathy (PHO) and chronic enteropathy associated with the SLCO2A1 gene (CEAS). Although the biophysical and biochemical properties of SLCO2A1 have been characterized, the precise mechanism by which SLCO2A1 recognizes and transports PGs remains unclear. Here, we present the cryo-electron microscopy structures of human SLCO2A1 in apo and PGE-bound forms, revealing the detailed structural features and structural basis for PGs transport. Fatty acid-like PGE binds in the central cavity, engaging in specific interactions with W565 and two serine residues, which are not conserved in other OATPs. Combined with functional assays and structural comparisons, this study offers mechanistic insights into PGE recognition, substrate selectivity, conformational changes, and pathology of SLCO2A1. PubMed: 40885756DOI: 10.1038/s41467-025-63615-8 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.2 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






