1A7B
ENGINEERING A MISFOLDED FORM OF CD2
1A7B の概要
| エントリーDOI | 10.2210/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: 9731771DOI: 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) |
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