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@ARTICLE{AyyappanJaguvaVasudevan:885798,
      author       = {Ayyappan Jaguva Vasudevan, Ananda and Balakrishnan, Kannan
                      and Gertzen, Christoph and Borvető, Fanni and Zhang, Zeli
                      and Sangwiman, Anucha and Held, Ulrike and Küstermann,
                      Caroline and Banerjee, Sharmistha and Schumann, Gerald G.
                      and Häussinger, Dieter and Bravo, Ignacio G. and Gohlke,
                      Holger and Münk, Carsten},
      title        = {{L}oop 1 of {APOBEC}3{C} regulates its antiviral activity
                      against {HIV}-1},
      journal      = {Journal of molecular biology},
      volume       = {432},
      number       = {23},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2020-04095},
      pages        = {6200-6227},
      year         = {2020},
      abstract     = {APOBEC3 deaminases (A3s) provide mammals with an
                      anti-retroviral barrier by catalyzing dC-to-dU deamination
                      on viral ssDNA. Within primates, A3s have undergone a
                      complex evolution via gene duplications, fusions, arms race
                      and selection. Human APOBEC3C (hA3C) efficiently restricts
                      the replication of viral infectivity factor (vif)-deficient
                      Simian immunodeficiency virus (SIVΔvif), but for unknown
                      reasons, it inhibits HIV-1Δvif only weakly. In catarrhines
                      (Old World monkeys and apes), the A3C loop 1 displays the
                      conserved amino acid pair WE, while the corresponding
                      consensus sequence in A3F and A3D is the largely divergent
                      pair RK, which is also the inferred ancestral sequence for
                      the last common ancestor of A3C and of the C-terminal
                      domains of A3D and A3F in primates. Here, we report that
                      modifying the WE residues in hA3C loop 1 to RK leads to
                      stronger interactions with substrate ssDNA, facilitating
                      catalytic function, which results in a drastic increase in
                      both deamination activity and in the ability to restrict
                      HIV-1 and LINE-1 replication. Conversely, the modification
                      $hA3F_WE$ resulted only in a marginal decrease in HIV-1Δvif
                      inhibition. We propose that the two series of ancestral gene
                      duplications that generated A3C, A3D-CTD and A3F-CTD allowed
                      neo/subfunctionalization: A3F-CTD maintained the ancestral
                      RK residues in loop 1, while diversifying selection resulted
                      in the RK→WE modification in Old World anthropoids’ A3C,
                      possibly allowing for novel substrate specificity and
                      function.},
      cin          = {JSC / NIC / IBI-7},
      ddc          = {610},
      cid          = {I:(DE-Juel1)JSC-20090406 / I:(DE-Juel1)NIC-20090406 /
                      I:(DE-Juel1)IBI-7-20200312},
      pnm          = {511 - Computational Science and Mathematical Methods
                      (POF3-511) / Forschergruppe Gohlke $(hkf7_20200501)$ / DFG
                      project 417919780 - Zentrum für strukturelle Studien},
      pid          = {G:(DE-HGF)POF3-511 / $G:(DE-Juel1)hkf7_20200501$ /
                      G:(GEPRIS)417919780},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:33068636},
      UT           = {WOS:000597938800016},
      doi          = {10.1016/j.jmb.2020.10.014},
      url          = {https://juser.fz-juelich.de/record/885798},
}