2M0R
Solution structure and dynamics of human S100A14
2M0R の概要
| エントリーDOI | 10.2210/pdb2m0r/pdb |
| NMR情報 | BMRB: 18818 |
| 分子名称 | Protein S100-A14 (1 entity in total) |
| 機能のキーワード | ef-hand proteins, protein dynamics, metal binding protein |
| 由来する生物種 | Homo sapiens (human) |
| 細胞内の位置 | Cytoplasm: Q9HCY8 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 23354.17 |
| 構造登録者 | Bertini, I.,Borsi, V.,Cerofolini, L.,Das Gupta, S.,Fragai, M.,Luchinat, C. (登録日: 2012-11-05, 公開日: 2013-01-23, 最終更新日: 2024-05-15) |
| 主引用文献 | Bertini, I.,Borsi, V.,Cerofolini, L.,Das Gupta, S.,Fragai, M.,Luchinat, C. Solution structure and dynamics of human S100A14. J.Biol.Inorg.Chem., 18:183-194, 2013 Cited by PubMed Abstract: Human S100A14 is a member of the EF-hand calcium-binding protein family that has only recently been described in terms of its functional and pathological properties. The protein is overexpressed in a variety of tumor cells and it has been shown to trigger receptor for advanced glycation end products (RAGE)-dependent signaling in cell cultures. The solution structure of homodimeric S100A14 in the apo state has been solved at physiological temperature. It is shown that the protein does not bind calcium(II) ions and exhibits a "semi-open" conformation that thus represents the physiological structure of the S100A14. The lack of two ligands in the canonical EF-hand calcium(II)-binding site explains the negligible affinity for calcium(II) in solution, and the exposed cysteines and histidine account for the observed precipitation in the presence of zinc(II) or copper(II) ions. PubMed: 23197251DOI: 10.1007/s00775-012-0963-3 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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