3O3U

Crystal Structure of Human Receptor for Advanced Glycation Endproducts (RAGE)

3O3U の概要

• エントリーDOI: 10.2210/pdb3o3u/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900009
• 分子名称: Maltose-binding periplasmic protein, Advanced glycosylation end product-specific receptor, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: rage, ager, scavenger receptor, macrophage cell surface receptor, innate immune receptor, ig fold, cell surface receptor, advanced glycation end products, age, amphoterin, s100b, s100a12, membrane, sugar transport, transport, transport protein, signaling protein
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 64034.51

構造登録者

Park, H.,Boyington, J.C. (登録日: 2010-07-26, 公開日: 2010-10-13, 最終更新日: 2024-11-27)

主引用文献

Park, H.,Boyington, J.C.
The 1.5 A crystal structure of human receptor for advanced glycation endproducts (RAGE) ectodomains reveals unique features determining ligand binding.
J.Biol.Chem., 285:40762-40770, 2010

PubMed Abstract: Interaction of the pattern recognition receptor, RAGE with key ligands such as advanced glycation end products (AGE), S100 proteins, amyloid β, and HMGB1 has been linked to diabetic complications, inflammatory and neurodegenerative disorders, and cancer. To help answer the question of how a single receptor can recognize and respond to a diverse set of ligands we have investigated the structure and binding properties of the first two extracellular domains of human RAGE, which are implicated in various ligand binding and subsequent signaling events. The 1.5-Å crystal structure reveals an elongated molecule with a large basic patch and a large hydrophobic patch, both highly conserved. Isothermal titration calorimetry (ITC) and deletion experiments indicate S100B recognition by RAGE is an entropically driven process involving hydrophobic interaction that is dependent on Ca(2+) and on residues in the C'D loop (residues 54-67) of domain 1. In contrast, competition experiments using gel shift assays suggest that RAGE interaction with AGE is driven by the recognition of negative charges on AGE-proteins. We also demonstrate that RAGE can bind to dsDNA and dsRNA. These findings reveal versatile structural features of RAGE that help explain its ability to recognize of multiple ligands.

PubMed: 20943659
DOI: 10.1074/jbc.M110.169276

実験手法

X-RAY DIFFRACTION (1.497 Å)