Skip to main content
. Author manuscript; available in PMC: 2019 Jan 5.
Published in final edited form as: Science. 2017 Oct 12;358(6366):1064–1068. doi: 10.1126/science.aao5154

Fig. 3. TAPBPR remodels the Dd73C binding groove.

Fig. 3.

(A to C) Superposition of the platform domain of Dd73C in the unliganded (gray) and TAPBPR-bound (blue) forms.TAPBPR is shown in pink. Groove widening at the α2–1 helix is indicated by arrows in (B) and (C). (D) Comparison of the floor of the peptide- binding groove of Dd73C in the unliganded (gray) and TAPBPR-bound (blue) forms. Movement of the β strands is depicted the arrow. (E) Contact between Y84 in the a1 helix of Dd73C (blue) and E102 of TAPBPR (pink). (F) Y84 of the Dd73C-5mer (gray) contacts a GL dipeptide (light blue) in the F pocket in the absence of TAPBPR. (G) Steric blocking of the A and B pockets of Dd73C in the TAPBPR-bound form by side-chain interactions between R66 and Y159. Electron density for these residues is depicted in dark blue. (H) Disposition of R66 and Y159 in the unliganded Dd73C-5mer when the groove is occupied by a peptide.