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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

IMPACT FACTOR 2017: 3.022

CiteScore 2017: 2.81

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Volume 394, Issue 11


Structural features of antiviral DNA cytidine deaminases

Ananda Ayyappan Jaguva Vasudevan
  • Clinic for Gastroenterology, Hepatology, and Infectiology, Medical Faculty, Heinrich-Heine-University, D-40225 Düsseldorf, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Sander H.J. Smits / Astrid Höppner / Dieter Häussinger
  • Clinic for Gastroenterology, Hepatology, and Infectiology, Medical Faculty, Heinrich-Heine-University, D-40225 Düsseldorf, Germany
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  • De Gruyter OnlineGoogle Scholar
/ Bernd W. Koenig
  • Institute of Structural Biochemistry (ICS-6), Research Centre Jülich, D-52425 Jülich, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Carsten Münk
  • Corresponding author
  • Clinic for Gastroenterology, Hepatology, and Infectiology, Medical Faculty, Heinrich-Heine-University, D-40225 Düsseldorf, Germany
  • Email
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2013-06-20 | DOI: https://doi.org/10.1515/hsz-2013-0165


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.

Keywords: APOBEC3G; HIV-1; homology modeling; NMR; Vif; X-ray


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About the article

Corresponding author: Carsten Münk, Clinic for Gastroenterology, Hepatology, and Infectiology, Medical Faculty, Heinrich-Heine-University, D-40225 Düsseldorf, Germany, e-mail:

Received: 2013-04-30

Accepted: 2013-06-17

Published Online: 2013-06-20

Published in Print: 2013-11-01

Citation Information: Biological Chemistry, Volume 394, Issue 11, Pages 1357–1370, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/hsz-2013-0165.

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Ananda Ayyappan Jaguva Vasudevan, Ulrike Kreimer, Wolfgang A. Schulz, Aikaterini Krikoni, Gerald G. Schumann, Dieter Häussinger, Carsten Münk, and Wolfgang Goering
Frontiers in Microbiology, 2018, Volume 9
Tatsuya Matsuoka, Takayuki Nagae, Hirotaka Ode, Hiroaki Awazu, Teppei Kurosawa, Akiko Hamano, Kazuhiro Matsuoka, Atsuko Hachiya, Mayumi Imahashi, Yoshiyuki Yokomaku, Nobuhisa Watanabe, and Yasumasa Iwatani
Nucleic Acids Research, 2018
Axel V. Horn, Sabine Klawitter, Ulrike Held, André Berger, Ananda Ayyappan Jaguva Vasudevan, Anja Bock, Henning Hofmann, Kay-Martin O. Hanschmann, Jan-Hendrik Trösemeier, Egbert Flory, Robert A. Jabulowsky, Jeffrey S. Han, Johannes Löwer, Roswitha Löwer, Carsten Münk, and Gerald G. Schumann
Nucleic Acids Research, 2014, Volume 42, Number 1, Page 396
D. V. Sosin and N. A. Tchurikov
Molecular Biology, 2017, Volume 51, Number 4, Page 483
Ananda Ayyappan Jaguva Vasudevan, Henning Hofmann, Dieter Willbold, Dieter Häussinger, Bernd W. Koenig, and Carsten Münk
Journal of Molecular Biology, 2017, Volume 429, Number 8, Page 1171
Daniela Marino, Mario Perković, Anika Hain, Ananda A. Jaguva Vasudevan, Henning Hofmann, Kay-Martin Hanschmann, Michael D. Mühlebach, Gerald G. Schumann, Renate König, Klaus Cichutek, Dieter Häussinger, Carsten Münk, and Javier Marcelo Di Noia
PLOS ONE, 2016, Volume 11, Number 6, Page e0155422
Tao Sun, Stephane Bentolila, and Maureen R. Hanson
Trends in Plant Science, 2016, Volume 21, Number 11, Page 962
Zeli Zhang, Qinyong Gu, Ananda Ayyappan Jaguva Vasudevan, Anika Hain, Björn-Philipp Kloke, Sascha Hasheminasab, Daniel Mulnaes, Kei Sato, Klaus Cichutek, Dieter Häussinger, Ignacio G. Bravo, Sander H. J. Smits, Holger Gohlke, and Carsten Münk
Retrovirology, 2016, Volume 13, Number 1
Fengchao Xu, Hongxiao Song, Na Li, and Guangyun Tan
Biochemical and Biophysical Research Communications, 2016, Volume 473, Number 1, Page 219
Andranik Ivanov, Sebastian Memczak, Emanuel Wyler, Francesca Torti, Hagit T. Porath, Marta R. Orejuela, Michael Piechotta, Erez Y. Levanon, Markus Landthaler, Christoph Dieterich, and Nikolaus Rajewsky
Cell Reports, 2015, Volume 10, Number 2, Page 170
Marek Widera, Frank Hillebrand, Steffen Erkelenz, Ananda Ayyappan Jaguva Vasudevan, Carsten Münk, and Heiner Schaal
Retrovirology, 2014, Volume 11, Number 1
Smita Nair and Alan Rein
Virus Research, 2014, Volume 193, Page 130
Bharat Vaidyanathan, Wei-Feng Yen, Joseph N. Pucella, and Jayanta Chaudhuri
Frontiers in Immunology, 2014, Volume 5

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