Fig. 3: The IN tetramer undergoes compression and domain rearrangements to assemble the hexadecameric HIV-1 intasome. | Nature Communications

Fig. 3: The IN tetramer undergoes compression and domain rearrangements to assemble the hexadecameric HIV-1 intasome.

From: Oligomeric HIV-1 integrase structures reveal functional plasticity for intasome assembly and RNA binding

Fig. 3

a Composite map of the complete HIV-1 intasome with four IN tetramers assembled with two vDNA ends. Each of four IN protomers are colored in red, orange, blue, or cyan; the vDNA is in gray. b Two distinct IN tetramers from the hexadecameric HIV-1 intasome are displayed as isosurfaces (left) and with the apo IN tetramer docked into the density (right). The two IN dimers constituting the apo tetramer must move closer together, or compress, to fit into each of the tetrameric building blocks within the HIV-1 intasome. This is apparent from the bottom dimer, which resides outside of the EM density, whereas the top dimer nearly perfectly superimposes. The curved arrows indicate rearrangements of NTDs and CTDs. c Schematic showing all major structural changes of the HIV-1 IN tetramer to accommodate intasome assembly. Boxes around the CCDs highlight the compression of individual IN dimers, whereas the curved arrows indicate rearrangements of NTDs and CTDs.

Back to article page