5XTW

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

5XTW の概要

• エントリーDOI: 10.2210/pdb5xtw/pdb
• 分子名称: Macrophage mannose receptor 1, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, CALCIUM ION (3 entities in total)
• 機能のキーワード: collagen binding, lectin-activity, endocytic receptor, immune receptor, sugar binding protein
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Endosome membrane ; Single-pass type I membrane protein : P22897
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 437105.68

構造登録者

He, Y.,Hu, Z. (登録日: 2017-06-21, 公開日: 2017-12-27, 最終更新日: 2023-11-22)

主引用文献

Hu, Z.,Shi, X.,Yu, B.,Li, N.,Huang, Y.,He, Y.
Structural Insights into the pH-Dependent Conformational Change and Collagen Recognition of the Human Mannose Receptor
Structure, 26:60-71.e3, 2018

PubMed Abstract: Mannose receptor (MR, CD206) is an endocytic receptor on microphages and dendritic cells. It recognizes multiple ligands and plays important roles in regulating immune responses and maintaining glycoprotein homeostasis. However, the structure and functional mechanism of MR remain unclear. Here we determine the crystal structures of the N-terminal fragments of MR and reveal the potential binding mode of collagen on the fibronectin II domain. The SAXS and other biophysical data suggest that MR adopts an extended conformation at physiological pH and undergoes conformational changes as pH decreases, resulting in a compact conformation in an acidic environment. Moreover, biochemical data show that MR binds to collagen in a Ca-enhanced manner at physiological pH, whereas Ca has no effect on the binding at acidic pH. These results provide a model for the dynamic mechanism of MR regarding its ligand binding and release during the recycling between cell surface and endosomes.

PubMed: 29225077
DOI: 10.1016/j.str.2017.11.006

実験手法

X-RAY DIFFRACTION (3.2 Å)