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@ARTICLE{Vasudevan:139785,
      author       = {Vasudevan, Ananda Ayyappan Jaguva and Smits, Sander H. J.
                      and Höppner, Astrid and Häussinger, Dieter and Münk,
                      Carsten and König, Bernd},
      title        = {{S}tructural features of antiviral {DNA} cytidine
                      deaminases},
      journal      = {Biological chemistry},
      volume       = {394},
      number       = {11},
      issn         = {1431-6730},
      address      = {Berlin [u.a.]},
      publisher    = {de Gruyter},
      reportid     = {FZJ-2013-05757},
      pages        = {1357 - 1370},
      year         = {2013},
      note         = {Bitte POF III Topic noch nachtragen.},
      abstract     = {The APOBEC3 (A3) family of cytidine deaminases plays a
                      vital role for innate defense against retroviruses.
                      Lentiviruses such as HIV-1 evolved the Vif protein that
                      triggers A3 protein degradation. There are seven A3
                      proteins, A3A-A3H, found in humans. All A3 proteins can
                      deaminate cytidines to uridines in single-stranded DNA
                      (ssDNA), generated during viral reverse transcription. A3
                      proteins have either one or two cytidine deaminase domains
                      (CD). The CDs coordinate a zinc ion, and their amino acid
                      specificity classifies the A3s into A3Z1, A3Z2, and A3Z3. A3
                      proteins occur as monomers, dimers, and large oligomeric
                      complexes. Studies on the nature of A3 oligomerization, as
                      well as the mode of interaction of A3s with RNA and ssDNA
                      are partially controversial. High-resolution structures of
                      the catalytic CD2 of A3G and A3F as well as of the single CD
                      proteins A3A and A3C have been published recently. The NMR
                      and X-ray crystal structures show globular proteins with six
                      α-helices and five β sheets arranged in a characteristic
                      motif (α1-β1-β2/2'-α2-β3-α3-β4-α4-β5-α5-α6).
                      However, the detailed arrangement and extension of
                      individual structure elements and their relevance for A3
                      complex formation and activity remains a matter of debate
                      and will be highlighted in this review.},
      cin          = {ICS-6},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000325717100002},
      pubmed       = {pmid:23787464},
      doi          = {10.1515/hsz-2013-0165},
      url          = {https://juser.fz-juelich.de/record/139785},
}