2N8I
Solution NMR Structure of Designed Protein DA05, Northeast Structural Genomics Consortium (NESG) Target OR626
2N8I の概要
| エントリーDOI | 10.2210/pdb2n8i/pdb |
| 関連するPDBエントリー | 2N8W |
| NMR情報 | BMRB: 25850 |
| 分子名称 | Designed Protein DA05 (1 entity in total) |
| 機能のキーワード | designed protein, de novo protein, psi-biology, northeast structural genomics consortium, nesg |
| 由来する生物種 | synthetic construct (artificial gene) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 11148.56 |
| 構造登録者 | Xu, X.,Eletsky, A.,Federizon, J.F.,Jacobs, T.M.,Kuhlman, B.,Szyperski, T.,Northeast Structural Genomics Consortium (NESG) (登録日: 2015-10-15, 公開日: 2016-01-20, 最終更新日: 2024-05-15) |
| 主引用文献 | Jacobs, T.M.,Williams, B.,Williams, T.,Xu, X.,Eletsky, A.,Federizon, J.F.,Szyperski, T.,Kuhlman, B. Design of structurally distinct proteins using strategies inspired by evolution. Science, 352:687-690, 2016 Cited by PubMed Abstract: Natural recombination combines pieces of preexisting proteins to create new tertiary structures and functions. We describe a computational protocol, called SEWING, which is inspired by this process and builds new proteins from connected or disconnected pieces of existing structures. Helical proteins designed with SEWING contain structural features absent from other de novo designed proteins and, in some cases, remain folded at more than 100°C. High-resolution structures of the designed proteins CA01 and DA05R1 were solved by x-ray crystallography (2.2 angstrom resolution) and nuclear magnetic resonance, respectively, and there was excellent agreement with the design models. This method provides a new strategy to rapidly create large numbers of diverse and designable protein scaffolds. PubMed: 27151863DOI: 10.1126/science.aad8036 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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