1AR2
DISULFIDE-FREE IMMUNOGLOBULIN FRAGMENT
1AR2 の概要
| エントリーDOI | 10.2210/pdb1ar2/pdb |
| 分子名称 | REI (2 entities in total) |
| 機能のキーワード | disulfide-free, immunoglobulin fragment, bence-jones, immunoglobulin |
| 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 | 11921.17 |
| 構造登録者 | Uson, I.,Bes, M.T.,Sheldrick, G.M.,Schneider, T.R.,Hartsch, T.,Fritz, H.-J. (登録日: 1997-08-08, 公開日: 1997-11-12, 最終更新日: 2024-05-22) |
| 主引用文献 | Uson, I.,Bes, M.T.,Sheldrick, G.M.,Schneider, T.R.,Hartsch, T.,Fritz, H.J. X-ray crystallography reveals stringent conservation of protein fold after removal of the only disulfide bridge from a stabilized immunoglobulin variable domain. Structure Fold.Des., 2:357-361, 1997 Cited by PubMed Abstract: Immunoglobulin domains owe a crucial fraction of their conformational stability to an invariant central disulfide bridge, the closure of which requires oxidation. Under the reducing conditions prevailing in cell cytoplasm, accumulation of soluble immunoglobulin is prohibited by its inability to acquire and maintain the native conformation. Previously, we have shown that disulfide-free immunoglobulins can be produced in Escherichia coli and purified from cytoplasmic extracts. PubMed: 9427009DOI: 10.1016/S1359-0278(97)00049-7 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.8 Å) |
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