1WO6
Solution structure of Designed Functional Finger 5 (DFF5): Designed mutant based on non-native CHANCE domain
Summary for 1WO6
Entry DOI | 10.2210/pdb1wo6/pdb |
Related | 1LIQ 1WO3 1WO4 1WO5 1WO7 |
NMR Information | BMRB: 6326 |
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 | 2736.57 |
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 Cited by 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: 15698569DOI: 10.1016/j.str.2004.12.007 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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