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. 2014 Dec 23;10(3):652–666. doi: 10.1021/cb500860x

Figure 4.

Figure 4

Structures of phosphorylated mRNA decay factors that bind 14–3–3 or 14–3–3-like domains. (A) Schematic showing domain organization of KSRP. The four KH domains are shown in red and the nuclear localization signals are in blue. (B) Solution NMR structure of the first KH domain (PDB code 2OPU) of KSRP when unphosphorylated. The site of phosphorylation, Ser193, is shown in stick. (C) Comparison of the folding topologies of 14–3–3ζ with 14–3–3-like domains from SMG6, SMG7, and the SMG5-SMG7 complex is shown in purple. The phosphoserine binding site is indicated. (D) Interaction of a phosphoserine peptide with 14–3–3ζ as seen in the crystal structure of the cocomplex (PDB code 1QJB) is depicted. The phosphoserine binds in an extended conformation to 14–3–3 proteins.