2P6J

Full-sequence computational design and solution structure of a thermostable protein variant

2P6J の概要

• エントリーDOI: 10.2210/pdb2p6j/pdb
• NMR情報: BMRB: 7401
• 分子名称: designed engrailed homeodomain variant UVF (1 entity in total)
• 機能のキーワード: de novo protein, helix-turn-helix, computational protein design, engrailed homeodomain
• 由来する生物種: unidentified
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6605.41

構造登録者

Shah, P.S.,Hom, G.K.,Ross, S.A.,Lassila, J.K.,Crowhurst, K.A.,Mayo, S.L. (登録日: 2007-03-18, 公開日: 2007-08-14, 最終更新日: 2024-05-22)

主引用文献

Shah, P.S.,Hom, G.K.,Ross, S.A.,Lassila, J.K.,Crowhurst, K.A.,Mayo, S.L.
Full-sequence Computational Design and Solution Structure of a Thermostable Protein Variant.
J.Mol.Biol., 372:1-6, 2007

PubMed Abstract: Computational protein design procedures were applied to the redesign of the entire sequence of a 51 amino acid residue protein, Drosophila melanogaster engrailed homeodomain. Various sequence optimization algorithms were compared and two resulting designed sequences were experimentally evaluated. The two sequences differ by 11 mutations and share 22% and 24% sequence identity with the wild-type protein. Both computationally designed proteins were considerably more stable than the naturally occurring protein, with midpoints of thermal denaturation greater than 99 degrees C. The solution structure was determined for one of the two sequences using multidimensional heteronuclear NMR spectroscopy, and the structure was found to closely match the original design template scaffold.

PubMed: 17628593
DOI: 10.1016/j.jmb.2007.06.032

実験手法

SOLUTION NMR