5J0H
De novo design of protein homo-oligomers with modular hydrogen bond network-mediated specificity
5J0H の概要
| エントリーDOI | 10.2210/pdb5j0h/pdb |
| 分子名称 | Design construct 2L6HC3_13 (2 entities in total) |
| 機能のキーワード | rosetta, de novo design, de novo protein |
| 由来する生物種 | synthetic construct |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 18286.83 |
| 構造登録者 | Sankaran, B.,Zwart, P.H.,Pereira, J.H.,Baker, D.,Boyken, S.,Chen, Z.,Groves, B.,Langan, R.A.,Oberdorfer, G.,Ford, A.,Gilmore, J.,Xu, C.,DiMaio, F.,Seelig, G. (登録日: 2016-03-28, 公開日: 2016-05-25, 最終更新日: 2024-03-06) |
| 主引用文献 | Boyken, S.E.,Chen, Z.,Groves, B.,Langan, R.A.,Oberdorfer, G.,Ford, A.,Gilmore, J.M.,Xu, C.,DiMaio, F.,Pereira, J.H.,Sankaran, B.,Seelig, G.,Zwart, P.H.,Baker, D. De novo design of protein homo-oligomers with modular hydrogen-bond network-mediated specificity. Science, 352:680-687, 2016 Cited by PubMed Abstract: In nature, structural specificity in DNA and proteins is encoded differently: In DNA, specificity arises from modular hydrogen bonds in the core of the double helix, whereas in proteins, specificity arises largely from buried hydrophobic packing complemented by irregular peripheral polar interactions. Here, we describe a general approach for designing a wide range of protein homo-oligomers with specificity determined by modular arrays of central hydrogen-bond networks. We use the approach to design dimers, trimers, and tetramers consisting of two concentric rings of helices, including previously not seen triangular, square, and supercoiled topologies. X-ray crystallography confirms that the structures overall, and the hydrogen-bond networks in particular, are nearly identical to the design models, and the networks confer interaction specificity in vivo. The ability to design extensive hydrogen-bond networks with atomic accuracy enables the programming of protein interaction specificity for a broad range of synthetic biology applications; more generally, our results demonstrate that, even with the tremendous diversity observed in nature, there are fundamentally new modes of interaction to be discovered in proteins. PubMed: 27151862DOI: 10.1126/science.aad8865 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.64 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






