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Figure 2


Fig. 2. Mutations in Tud domains may affect interactions with polar granule components. (A-C) Structures of (A) Tud domain 10 and (B) Tud domain 1 were predicted based on (C) the known structure of the Tud domain from the Smn protein (Selenko et al., 2001; Sprangers et al., 2003). (A') Predicted structure of Tud domain 10 with an Arg2228Cys change. (B') Predicted structure of Tud domain 1 with an Arg91Trp change. Arg, Cys and Trp residues in Tud domains 1 and 10, and the corresponding Pro residue in the Smn Tud domain, are shown in magenta. Glu134 of the Smn Tud domain plays a crucial role in protein-protein interactions (Selenko et al., 2001) and is indicated in green. The cluster of aromatic amino acids, which form a binding pocket for the Smn Tud domain interacting partners, is shown in yellow.





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