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Figure 4 | Arthritis Res Ther

Figure 4

From: The tandem CCCH zinc finger protein tristetraprolin and its relevance to cytokine mRNA turnover and arthritis

Figure 4

Proposed structure of the human tristetraprolin (TTP) tandem zinc finger domain in complex with the TTP-binding site 5'-UUAUUUAUU-3'. This proposed structure was modeled on the original nuclear magnetic resonance structure described by [32], using their pdb coordinates and the Swiss-Model program. The RNA oligonucleotide is shown in magenta, with the 5' and 3' ends indicated, along with the key residues A3, U5, and A7. The peptide is shown as a surface structure, with the buried zinc residues highlighted and the amino-terminal (N-term.) and carboxy-terminal (C-term.) ends of the peptide shown by arrows. The dark blue residues represent amino acids that are identical between human TTP and the ZFP36L2 (TIS11D) protein used in the original structure. The other colors represent progressively greater amino acid differences between the two proteins, ranging from minimally different (aquamarine, upper right), through green, yellow, and orange, with orange representing the most marked amino acid differences.

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