1WO5

Solution structure of Designed Functional Finger 2 (DFF2): Designed mutant based on non-native CHANCE domain

Summary for 1WO5

• Entry DOI: 10.2210/pdb1wo5/pdb
• Related: 1LIQ 1WO3 1WO4 1WO6 1WO7
• NMR Information: BMRB: 6327
• Descriptor: CREB Binding Protein, ZINC ION (2 entities in total)
• Functional Keywords: zinc finger, protein design, transferase
• Cellular location: Cytoplasm: Q92793
• Total number of polymer chains: 1
• Total formula weight: 2670.61

Authors

Sharpe, B.K.,Liew, C.K.,Wilce, J.A.,Crossley, M.,Matthews, J.M.,Mackay, J.P. (deposition date: 2004-08-12, release date: 2005-03-08, Last modification date: 2024-05-29)

Primary citation

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

Experimental method

SOLUTION NMR