Author: Meytal Galilee; Akram Alian
Title: Multimerization of HIV-1 integrase hinges on conserved SH3-docking platforms Document date: 2018_4_16
ID: 4fuxbte0_6
Snippet: Within a functional IN tetramer, the NTD and CTD of one dimer wrap around an extended α-helix (α4) of CCD of a second dimer ( Figure 1B) , an interdomaindocking platform that is functionally imperative (9) . Previously, we showed that complementarity-defining regions 3 (CDR3) and 2 (CDR2) of an anti-IN Fab wrap around α4 of IN CCD (residues 153-168) and dock into a cleft rimmed by the CCD finger loop (residues 186-191) ( Figure 1C ). We deriv.....
Document: Within a functional IN tetramer, the NTD and CTD of one dimer wrap around an extended α-helix (α4) of CCD of a second dimer ( Figure 1B) , an interdomaindocking platform that is functionally imperative (9) . Previously, we showed that complementarity-defining regions 3 (CDR3) and 2 (CDR2) of an anti-IN Fab wrap around α4 of IN CCD (residues 153-168) and dock into a cleft rimmed by the CCD finger loop (residues 186-191) ( Figure 1C ). We derived a peptide (WSYFYDGSYSYYDYESY) mostly representing the CDR3 sequence (underlined) with the addition of Trp (for UV-Vis absorbance) and Ser-Tyr (representing CDR2 extension in wrapping around α4). Similar to parental Fab, the peptide inhibited IN strand-transfer activity but not 3'processing ( Figure 1D ), suggesting potential interference with IN functional multimerization.
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