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. Author manuscript; available in PMC: 2019 Dec 1.
Published in final edited form as: Trends Genet. 2018 Oct 10;34(12):972–990. doi: 10.1016/j.tig.2018.09.006

Figure 2. Structure and RNA recognition by PUM1 and PUM2.

Figure 2.

(A) High conservation of the RNA-binding surface of PUM proteins. Ribbon diagram of a crystal structure of human PUM1 in complex with hb NRE RNA is shown colored according to the degree of amino acid sequence conservation calculated using the Consurf server [117]. The most highly conserved positions are colored maroon, and the least conserved are colored cyan. The specific PUM1 amino acid residues that are mutated in PADDAS (R1139W and R1147W) and the PRCA (T1035S) are indicated by space-filling spheres. (B) PUM1 RNA recognition code. Specific interaction of Pum repeats with U, A, G, and C nucleotides is shown. (C) Ribbon diagram of a crystal structure of human PUM2 in complex with erk2 PRE RNA. The RNA-binding helices are colored maroon. PUM2 binds to the erk2 PRE RNA using the alternative ‘base-omission mode,’ where bases A4 and C5 (green) are directly stacked and R888 in repeat 5 (green) does not stack between bases A4 and C5.