Figure 5
From: Phosphotyrosine recognition domains: the typical, the atypical and the versatile
The structure and sequence conservation of the HYB domain. (A) The HYB domain is coordinated with six zinc ions. Shown is the homo-dimeric structure of the Hakai HYB domain (showing the two chains with different colours) (PDB ID: 3VK6) [96]. Zinc ions are depicted as spheres. The 24 residues (12 per monomer) coordinating the zinc ions are shown as green sticks. The four residues, His127, Tyr176, His185, and Arg189 from each monomer, identified as sticks, mainly contribute to pTyr binding by providing a positively charged pocket. (B) HYB domain-like sequences identified in animals and plants. The alignment was generated by the program MAFFT [130]. The 12 zinc-binding residues are shaded green, showing that all of them are strictly conserved within these species. The human Hakai HYB domain was aligned with following sequences with UniProt IDs: zebrafish (Q5RGV5), fruit fly (Q9VIT1), Arabidopsis thaliana (Q9LFC0), wine grape (F6HKX7), and Japanese rice (Q0IWQ6).