Selected article for: "activity inhibit and virus particle"
Author: Meytal Galilee; Akram Alian
Title: Multimerization of HIV-1 integrase hinges on conserved SH3-docking platforms
  • Document date: 2018_4_16
    • ID: 4fuxbte0_2
    Snippet: Tetramers of IN are formed by the reciprocal swapping of the three, N-terminal, catalytic core and Cterminal, canonical domains of IN. The two internal IN protomers, where catalytic binding of viral and host DNA takes place, make up the majority of the tetramer interface. The outer two protomers, and other surrounding units in higher order assemblies, provide supportive domains indispensible for the assembly of the tetrameric cores (4) (5) (6) (7.....
    Document: Tetramers of IN are formed by the reciprocal swapping of the three, N-terminal, catalytic core and Cterminal, canonical domains of IN. The two internal IN protomers, where catalytic binding of viral and host DNA takes place, make up the majority of the tetramer interface. The outer two protomers, and other surrounding units in higher order assemblies, provide supportive domains indispensible for the assembly of the tetrameric cores (4) (5) (6) (7) (8) . We recently showed that targeting the interface between the N-terminal domain (NTD) and catalytic core domain (CCD) of IN, using a specific antigen-binding fragment (Fab), inhibits IN tetramer formation and consequent enzymatic activity and virus particle production (9) . Disrupting the dimerization of the elementary dimeric blocks building IN tetramers has also been explored as a strategy to inhibit IN activity (15) .

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