6INV

Crystal structure of the CysR-CTLD2 fragment of human MR at acidic pH (pH 4.0)

6INV の概要

• エントリーDOI: 10.2210/pdb6inv/pdb
• 分子名称: Macrophage mannose receptor 1 (1 entity in total)
• 機能のキーワード: cd206, mannose receptor family, ph-dependent, conformational change, scavenger receptor, immune system
• 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: 54412.91

構造登録者

Hu, Z.,He, Y. (登録日: 2018-10-27, 公開日: 2019-09-18, 最終更新日: 2024-11-06)

主引用文献

Hu, Z.,Wang, Y.,Cheng, C.,He, Y.
Structural basis of the pH-dependent conformational change of the N-terminal region of human mannose receptor/CD206.
J.Struct.Biol., 208:107384-107384, 2019

PubMed Abstract: Mannose receptor (MR, CD206) is an immune receptor highly expressed on macrophages and plays important roles in glycoprotein clearance, immune response and matrix turnover. Previous studies have shown that MR recognizes multiple ligands and recycles between cell surface and endosomes, and the conformation and ligand binding of MR are regulated by environmental pH. However, due to the lack of high-resolution details, the mechanisms of the pH-dependent properties of MR have not been fully understood. Here we investigate the pH-dependent conformational change of MR by solving a series of crystal structures of MR N-terminal fragments (CysR~CTLD2/3) at pH ranging from 4.0 to 8.5. The results show that the CTLD3 domain plays a critical role in regulating the conformational change of the N-terminal region of MR by forming interactions with the CTLD2 domain specifically at acidic pH. Moreover, the structural data also show the conformational changes of the 4-SO-GalNAc binding pocket at the CysR domain, which might be relevant to the binding and release of the ligand. Overall, these results provide a model for the pH-dependent conformational change of the N-terminal region of MR that may help to understand its functional mechanism at molecular level.

PubMed: 31491467
DOI: 10.1016/j.jsb.2019.09.001

実験手法

X-RAY DIFFRACTION (3.3 Å)