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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

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Structural features of antiviral DNA cytidine deaminases

Ananda Ayyappan Jaguva Vasudevan1 / Sander H.J. Smits2 / Astrid Höppner3 / Dieter Häussinger1 / Bernd W. Koenig4 / 1

1Clinic for Gastroenterology, Hepatology, and Infectiology, Medical Faculty, Heinrich-Heine-University, D-40225 Düsseldorf, Germany

2Institute of Biochemistry, Heinrich-Heine-University, D-40225 Düsseldorf, Germany

3Crystal and X-Ray Facility, Heinrich-Heine-University, D-40225 Düsseldorf, Germany

4Institute of Structural Biochemistry (ICS-6), Research Centre Jülich, D-52425 Jülich, Germany

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

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

Publication History

Received:
2013-04-30
Accepted:
2013-06-17
Published Online:
2013-06-20

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.

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

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