Figure 4: Solid-state MAS NMR studies of the intermolecular interfaces formed between CypA and CA in CypA-CA complex assemblies.
From: Cyclophilin A stabilizes the HIV-1 capsid through a novel non-canonical binding site
(a) Expansions of 2D MAS NMR spectra of U-13C,15N-CA tubular assemblies, free (green) and in complex with CypA (black), acquired at 19.9 T. Top two panels: 13C-13C CORD, bottom two panels: 15N-13C NCACX. The peaks whose chemical shifts or intensities change in the presence of CypA are labelled. (b) Mapping of chemical shift and/or intensity changes onto the 3D structure of CA (PDB: 3NTE). Purple indicates residues whose shifts or intensities are perturbed. (c) Expansions of 2D MAS NMR spectra of CA/U-13C,15N-CypA assemblies acquired at 19.9 T. Top: 13C-13C CORD, bottom: 15N-13C NCA. The spectra are shown for the varying CypA:CA ratios: 1:4 (purple), and 1:2 (orange). The peaks whose chemical shifts or intensities change as a function of the CypA:CA ratios are labelled. (d) Mapping of chemical shift and/or intensity changes on the 3D structure of CypA. Red and yellow are the changes when the CypA:CA ratio is shifted from 1:4 to 1:2 and 1:2 to 1:1, respectively.
