2MN4

NMR solution structure of a computational designed protein based on structure template 1cy5

2MN4 の概要

• エントリーDOI: 10.2210/pdb2mn4/pdb
• 関連するPDBエントリー: 2MLB
• NMR情報: BMRB: 19879
• 分子名称: Computational designed protein based on structure template 1cy5 (1 entity in total)
• 機能のキーワード: protein design, statistical energy function, alpha-helical greek, protein evolution, de novo protein
• 由来する生物種: synthetic
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12403.27

構造登録者

Xiong, P.,Wang, M.,Zhang, J.,Chen, Q.,Liu, H. (登録日: 2014-03-28, 公開日: 2014-10-29, 最終更新日: 2024-05-15)

主引用文献

Xiong, P.,Wang, M.,Zhou, X.,Zhang, T.,Zhang, J.,Chen, Q.,Liu, H.
Protein design with a comprehensive statistical energy function and boosted by experimental selection for foldability
Nat Commun, 5:5330-5330, 2014

PubMed Abstract: The de novo design of amino acid sequences to fold into desired structures is a way to reach a more thorough understanding of how amino acid sequences encode protein structures and to supply methods for protein engineering. Notwithstanding significant breakthroughs, there are noteworthy limitations in current computational protein design. To overcome them needs computational models to complement current ones and experimental tools to provide extensive feedbacks to theory. Here we develop a comprehensive statistical energy function for protein design with a new general strategy and verify that it can complement and rival current well-established models. We establish that an experimental approach can be used to efficiently assess or improve the foldability of designed proteins. We report four de novo proteins for different targets, all experimentally verified to be well-folded, solved solution structures for two being in excellent agreement with respective design targets.

PubMed: 25345468
DOI: 10.1038/ncomms6330

実験手法

SOLUTION NMR