Additional file 1.

Neighboring residues of the tryptophans in tCWCH2 3D structure. (A) Distances of the tCWCH2-forming residues from the tCWCH2 ZF1 tryptophan (left) and the tCWCH2 ZF2 tryptophan (right). Black and red letters indicate residues in the ZF1 and the ZF2 respectively. Gothic letters, zinc chelating residue; *, ϕ1 and ϕ2 in Figure 5 and 6. Note that both tryptophan residues were close to the residues in the other C2H2 ZF unit. (B) Stereo view of the ZIC3, GLI1, and Zap1 tryptophan side chain adjacent residues within 5 Å. Tryptophan residues, zinc chelating histidine, ϕ1, and ϕ2 residues are labeled. For ZIC3 and Zap1, 20 NMR models in wire model are superimposed. For GLI1, cylinder model are shown. White, carbon; red, oxygen; blue, nitrogen; yellow; sulfur.

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Hatayama and Aruga BMC Evolutionary Biology 2010 10:53   doi:10.1186/1471-2148-10-53