TY  - JOUR
AU  - Vasudevan, Ananda Ayyappan Jaguva
AU  - Smits, Sander H. J.
AU  - Höppner, Astrid
AU  - Häussinger, Dieter
AU  - Münk, Carsten
AU  - König, Bernd
TI  - Structural features of antiviral DNA cytidine deaminases
JO  - Biological chemistry
VL  - 394
IS  - 11
SN  - 1431-6730
CY  - Berlin [u.a.]
PB  - de Gruyter
M1  - FZJ-2013-05757
SP  - 1357 - 1370
PY  - 2013
N1  - Bitte POF III Topic noch nachtragen.
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000325717100002
C6  - pmid:23787464
DO  - DOI:10.1515/hsz-2013-0165
UR  - https://juser.fz-juelich.de/record/139785
ER  -