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. Author manuscript; available in PMC: 2020 Apr 9.
Published in final edited form as: Curr Opin Struct Biol. 2019 Apr 9;55:50–58. doi: 10.1016/j.sbi.2019.03.002

Figure 3: Role of TRiC subunit diversity in substrate recognition and binding.

Figure 3:

(A) Structural model of apical domain of TRiC subunit CCT3 bound to substrate HIV protein p6. Helix 11 (and Proximal Loop make up binding domain, amino acid characteristics indicated by color: Nonpolar (yellow), Basic (blue), Acidic (red) and Polar (grey). (B) Top view of TRiC open conformation, which exposes the substrate binding regions of each apical domain. The Hx11/PL determinant is shown in spacefill following coloring scheme in (A), their differing characteristics allow polyvalent binding and diversity of substrate recognition. (C) The substrate binding region of apical domain (red) clashes with the RLS domain of its neighboring subunit (green) in the closed conformations, facilitates substrate release into the chamber.