4IW1
HSA-fructose complex
4IW1 の概要
エントリーDOI | 10.2210/pdb4iw1/pdb |
関連するPDBエントリー | 4IW2 |
分子名称 | Serum albumin, beta-D-fructofuranose, PHOSPHATE ION, ... (5 entities in total) |
機能のキーワード | heart shape, transport, 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 | 67026.50 |
構造登録者 | |
主引用文献 | Wang, Y.,Yu, H.,Shi, X.,Luo, Z.,Lin, D.,Huang, M. Structural mechanism of ring-opening reaction of glucose by human serum albumin J.Biol.Chem., 288:15980-15987, 2013 Cited by PubMed Abstract: Glucose reacts with proteins nonenzymatically under physiological conditions. Such glycation is exacerbated in diabetic patients with high levels of blood sugar and induces various complications. Human albumin serum (HSA) is the most abundant protein in plasma and is glycated by glucose. The glycation sites on HSA remain controversial among different studies. Here, we report two protein crystal structures of HSA in complex with either glucose or fructose. These crystal structures reveal the presence of linear forms of sugar for both monosaccharides. The linear form of glucose forms a covalent bond to Lys-195 of HSA, but this is not the case for fructose. Based on these structures, we propose a mechanism for glucose ring opening involving both residues Lys-195 and Lys-199. These results provide mechanistic insights to understand the glucose ring-opening reaction and the glycation of proteins by monosaccharides. PubMed: 23592780DOI: 10.1074/jbc.M113.467027 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.56 Å) |
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