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1AR2

DISULFIDE-FREE IMMUNOGLOBULIN FRAGMENT

1AR2 の概要
エントリーDOI10.2210/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: 9427009
DOI: 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)
構造検証レポート
Validation report summary of 1ar2
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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