3AQG
Crystal structure of human pancreatic secretory protein ZG16b
3AQG の概要
エントリーDOI | 10.2210/pdb3aqg/pdb |
関連するPDBエントリー | 3APA |
分子名称 | Zymogen granule protein 16 homolog B, PHOSPHATE ION (3 entities in total) |
機能のキーワード | beta-prism fold, unknown function |
由来する生物種 | Homo sapiens (human) |
細胞内の位置 | Secreted (Potential): Q96DA0 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 34933.06 |
構造登録者 | Kanagawa, M.,Satoh, T.,Nakano, Y.,Kojima-Aikawa, K.,Yamaguchi, Y. (登録日: 2010-11-01, 公開日: 2010-12-08, 最終更新日: 2023-11-01) |
主引用文献 | Kanagawa, M.,Satoh, T.,Ikeda, A.,Nakano, Y.,Yagi, H.,Kato, K.,Kojima-Aikawa, K.,Yamaguchi, Y. Crystal structures of human secretory proteins ZG16p and ZG16b reveal a Jacalin-related beta-prism fold Biochem.Biophys.Res.Commun., 2010 Cited by PubMed Abstract: ZG16p is a secretory protein that mediates condensation-sorting of pancreatic enzymes to the zymogen granule membrane in pancreatic acinar cells. ZG16p interacts with glycosaminoglycans and the binding is considered to be important for condensation-sorting of pancreatic enzymes. ZG16b/PAUF, a paralog of ZG16p, has recently been found to play a role in gene regulation and cancer metastasis. However, the detailed functions of ZG16p and ZG16b remain to be clarified. Here, in order to obtain insights into structure-function relationships, we conducted crystallographic studies of human ZG16p lectin as well as its paralog, ZG16b, and determined their crystal structures at 1.65 and 2.75 Å resolution, respectively. ZG16p has a Jacalin-related β-prism fold, the first to be reported among mammalian lectins. The putative sugar-binding site of ZG16p is occupied by a glycerol molecule, mimicking the mannose bound to Jacalin-related mannose-binding-type plant lectins such as Banlec. ZG16b also has a β-prism fold, but some amino acid residues of the putative sugar-binding site differ from those of the mannose-type binding site suggesting altered preference. A positively charged patch, which may bind sulfated groups of the glycosaminoglycans, is located around the putative sugar-binding site of ZG16p and ZG16b. Taken together, we suggest that the sugar-binding site and the adjacent basic patch of ZG16p and ZG16b cooperatively form a functional glycosaminoglycan-binding site. PubMed: 21110947DOI: 10.1016/j.bbrc.2010.11.093 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.75 Å) |
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