Figure 5. Interactions between NPF... | Rockefeller University Press

Figure 5.

Interactions between NPF surrounding residues and the EH2domain.(A) The αB and αC helices of EH2 were manually aligned with TM1 and H8 of rhodopsin, respectively. (B) Rotation of A by 90° to visualize the Gt binding surface of rhodopsin. Note that ICL1 of rhodopsin occupies a similar space as the αC–αB loop of the EH2 domain. (C) Closeup of B with rhodopsin removed and the STNPFR peptide shown in its binding orientation with the EH2 domain. (D) Comparison of the EH2 domain contacts with residues surrounding the NPF motif in the structures of the EH2 domain bound to PTGSSSTNPFR (PDB accession no. 1F8H) and the EH2 domain bound to PTGSSSTNPFL (PDB accession no. 1FF1). Residues from the αC–αB loop and αC helix that contact the residues surrounding the NPF motif are indicated in grey boxes; interacting residues were determined in PyMOL as any contact <4 Å. Contacts between residues at the −2 position, with respect to NPF, and αC–αB loop and αC helix are indicated by black lines; contacts between residues at the −1 position, with respect to NPF, and αC–αB loop and αC helix are indicated by purple lines; contacts between residues at the +1 position, with respect to NPF, and αC–αB loop and αC helix are indicated by green lines.

Interactions between NPF surrounding residues and the EH ₂ domain. (A) The αB and αC helices of EH₂ were manually aligned with TM1 and H8 of rhodopsin, respectively. (B) Rotation of A by 90° to visualize the Gt binding surface of rhodopsin. Note that ICL1 of rhodopsin occupies a similar space as the αC–αB loop of the EH₂ domain. (C) Closeup of B with rhodopsin removed and the STNPFR peptide shown in its binding orientation with the EH₂ domain. (D) Comparison of the EH₂ domain contacts with residues surrounding the NPF motif in the structures of the EH₂ domain bound to PTGSSSTNPFR (PDB accession no. 1F8H) and the EH₂ domain bound to PTGSSSTNPFL (PDB accession no. 1FF1). Residues from the αC–αB loop and αC helix that contact the residues surrounding the NPF motif are indicated in grey boxes; interacting residues were determined in PyMOL as any contact <4 Å. Contacts between residues at the −2 position, with respect to NPF, and αC–αB loop and αC helix are indicated by black lines; contacts between residues at the −1 position, with respect to NPF, and αC–αB loop and αC helix are indicated by purple lines; contacts between residues at the +1 position, with respect to NPF, and αC–αB loop and αC helix are indicated by green lines.