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1A7B

ENGINEERING A MISFOLDED FORM OF CD2

1A7B の概要
エントリーDOI10.2210/pdb1a7b/pdb
分子名称CD2 (1 entity in total)
機能のキーワードcd2, domain swapping, oligomerization, protein folding, protein evolution
由来する生物種Rattus norvegicus (Norway rat)
細胞内の位置Membrane; Single-pass type I membrane protein: P08921
タンパク質・核酸の鎖数4
化学式量合計43593.04
構造登録者
Murray, A.J.,Head, J.G.,Barker, J.J.,Brady, R.L. (登録日: 1998-03-10, 公開日: 1998-06-17, 最終更新日: 2024-05-22)
主引用文献Murray, A.J.,Head, J.G.,Barker, J.J.,Brady, R.L.
Engineering an intertwined form of CD2 for stability and assembly.
Nat.Struct.Biol., 5:778-782, 1998
Cited by
PubMed Abstract: The amino-terminal domain of CD2 has the remarkable ability to fold in two ways: either as a monomer or as an intertwined, metastable dimer. Here we show that it is possible to differentially stabilize either fold by engineering the CD2 sequence, mimicking random mutagenesis events that could occur during molecular evolution. Crystal structures of a hinge-deletion mutant, which is stable as an intertwined dimer, reveal domain rotations that enable the protein to further assemble to a tetramer. These results demonstrate that a variety of folds can be adopted by a single polypeptide sequence, and provide guidance for the design of proteins capable of further assembly.
PubMed: 9731771
DOI: 10.1038/1816
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.1 Å)
構造検証レポート
Validation report summary of 1a7b
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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