Backbone NMR Assignments of WW2 domain from human AIP4
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WW domains are small protein modules consisting of three-stranded antiparallel β-sheet, and involved in the protein-protein interaction for various biological systems. We overexpressed and purified WW2 domain from human AIP4/Itch (a member of Nedd4 family) using a pH/temperature dependent cleavage system. The backbone assignments of WW2 domain were completed, and secondary structure was predicted. Furthermore, backbone flexibility of WW2 domain was determined by 1H-15N heteronuclear NOE and amide hydrogen exchange experiments. The structural information would contribute to the structural determination of WW2 domain as well as the interaction study of WW2 domain with various binding partners.
Abstract
WW domains are small protein modules consisting of three-stranded antiparallel β-sheet, and involved in the protein-protein interaction for various biological systems. We overexpressed and purified WW2 domain from human AIP4/Itch (a member of Nedd4 family) using a pH/temperature dependent cleavage system. The backbone assignments of WW2 domain were completed, and secondary structure was predicted. Furthermore, backbone flexibility of WW2 domain was determined by 1H-15N heteronuclear NOE and amide hydrogen exchange experiments. The structural information would contribute to the structural determination of WW2 domain as well as the interaction study of WW2 domain with various binding partners.
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