1wo5
From Proteopedia
Solution structure of Designed Functional Finger 2 (DFF2): Designed mutant based on non-native CHANCE domain
Overview
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.
About this Structure
1WO5 is a Single protein structure. Full crystallographic information is available from OCA.
Reference
Assessment of the robustness of a serendipitous zinc binding fold: mutagenesis and protein grafting., Sharpe BK, Liew CK, Kwan AH, Wilce JA, Crossley M, Matthews JM, Mackay JP, Structure. 2005 Feb;13(2):257-66. PMID:15698569 Page seeded by OCA on Sat May 3 13:56:11 2008
