1WO3

Solution structure of Minimal Mutant 1 (MM1): Multiple alanine mutant of non-native CHANCE domain

1WO3 の概要

• エントリーDOI: 10.2210/pdb1wo3/pdb
• 関連するPDBエントリー: 1LIQ 1WO4 1WO5 1WO6 1WO7
• NMR情報: BMRB: 6329
• 分子名称: CREB Binding Protein, ZINC ION (2 entities in total)
• 機能のキーワード: zinc finger, protein design, transferase
• 細胞内の位置: Cytoplasm: Q92793
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2480.30

構造登録者

Sharpe, B.K.,Liew, C.K.,Wilce, J.A.,Crossley, M.,Matthews, J.M.,Mackay, J.P. (登録日: 2004-08-12, 公開日: 2005-03-08, 最終更新日: 2024-05-29)

主引用文献

Sharpe, B.K.,Liew, C.K.,Kwan, A.H.,Wilce, J.A.,Crossley, M.,Matthews, J.M.,Mackay, J.P.
Assessment of the robustness of a serendipitous zinc binding fold: mutagenesis and protein grafting
Structure, 13:257-266, 2005

PubMed Abstract: Zinc binding motifs have received much attention in the area of protein design. Here, we have tested the suitability of a recently discovered nonnative zinc binding structure as a protein design scaffold. A series of multiple alanine mutants was created to investigate the minimal requirements for folding, and solution structures of these mutants showed that the original fold was maintained, despite changes in approximately 50% of the sequence. We next attempted to transplant binding faces from chosen bimolecular interactions onto one of these mutants, and many of the resulting "chimeras" were shown to adopt a native-like fold. These results both highlight the robust nature of small zinc binding domains and underscore the complexity of designing functional proteins, even using such small, highly ordered scaffolds as templates.

PubMed: 15698569
DOI: 10.1016/j.str.2004.12.007

実験手法

SOLUTION NMR