8HNA

Crystal structure of N-terminal fragment (20-221aa) of human SCARF1

8HNA の概要

• エントリーDOI: 10.2210/pdb8hna/pdb
• 分子名称: Scavenger receptor class F member 1 (1 entity in total)
• 機能のキーワード: cell surface receptor, lipid binding 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: 23042.06

構造登録者

Wang, Y.,He, Y.,Li, G. (登録日: 2022-12-07, 公開日: 2023-12-20, 最終更新日: 2024-12-11)

主引用文献

Wang, Y.,Xu, F.,Li, G.,Cheng, C.,Yu, B.,Zhang, Z.,Kong, D.,Chen, F.,Liu, Y.,Fang, Z.,Cao, L.,Yu, Y.,Gu, Y.,He, Y.
Structure of scavenger receptor SCARF1 and its interaction with lipoproteins.
Elife, 13:-, 2024

PubMed Abstract: SCARF1 (scavenger receptor class F member 1, SREC-1 or SR-F1) is a type I transmembrane protein that recognizes multiple endogenous and exogenous ligands such as modified low-density lipoproteins (LDLs) and is important for maintaining homeostasis and immunity. But the structural information and the mechanisms of ligand recognition of SCARF1 are largely unavailable. Here, we solve the crystal structures of the N-terminal fragments of human SCARF1, which show that SCARF1 forms homodimers and its epidermal growth factor (EGF)-like domains adopt a long-curved conformation. Then, we examine the interactions of SCARF1 with lipoproteins and are able to identify a region on SCARF1 for recognizing modified LDLs. The mutagenesis data show that the positively charged residues in the region are crucial for the interaction of SCARF1 with modified LDLs, which is confirmed by making chimeric molecules of SCARF1 and SCARF2. In addition, teichoic acids, a cell wall polymer expressed on the surface of gram-positive bacteria, are able to inhibit the interactions of modified LDLs with SCARF1, suggesting the ligand binding sites of SCARF1 might be shared for some of its scavenging targets. Overall, these results provide mechanistic insights into SCARF1 and its interactions with the ligands, which are important for understanding its physiological roles in homeostasis and the related diseases.

PubMed: 39541158
DOI: 10.7554/eLife.93428

実験手法

X-RAY DIFFRACTION (2.6 Å)