GYF domains are conserved eukayotic adaptor domains that recognize proline-rich sequences. While the structure and function of the prototypic GYF domain from the human CD2BP2 protein has been characterized in detail, very little is known about GYF domains from other proteins and species. Here we describe the binding properties of four GYF domains of various origin. Phage display in combination with SPOT analysis revealed the PPG[F, I, L, M, V] motif as general recognition signature. Based on these results, the proteomes of human, yeast and A. thaliana were searched for potential interaction sites. Binding of several candidate proteins was confirmed by pulldown experiments or yeast two-hybrid analysis. The binding epitope of the GYF domain from the yeast SMY2 protein was mapped by NMR spectroscopy and lead to a structural model that accounts for the different binding properties of SMY2-type GYF domains and the CD2BP2-GYF domain.
|Evidence ID||Analyze ID||Interactor||Interactor Systematic Name||Interactor||Interactor Systematic Name||Type||Assay||Annotation||Action||Modification||Phenotype||Source||Reference||Note|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Gene Ontology Term||Gene Ontology Term ID||Qualifier||Aspect||Method||Evidence||Source||Assigned On||Reference||Annotation Extension|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Phenotype||Experiment Type||Experiment Type Category||Mutant Information||Strain Background||Chemical||Details||Reference|
|Evidence ID||Analyze ID||Regulator||Regulator Systematic Name||Target||Target Systematic Name||Experiment||Conditions||Strain||Source||Reference|