1wo5
Solution structure of Designed Functional Finger 2 (DFF2): Designed mutant based on non-native CHANCE domain
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OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Blue-cone monochromacy OMIM:[303900], Colorblindness, protan OMIM:[303900], Rubenstein-Taybi syndrome OMIM:[600140]
About this StructureAbout this Structure
1WO5 is a Single protein structure of sequence from [1] with ZN as ligand. Active as Histone acetyltransferase, with EC number 2.3.1.48 Full crystallographic information is available from OCA.
ReferenceReference
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 Mon Nov 12 19:52:53 2007