| BYEON, In-Ja L, Jinwoo AHN, Mithun MITRA, Chang-Hyeock BYEON, Kamil HERCIK, Jozef HRITZ, Lisa M CHARLTON, Judith G LEVIN and Angela M GRONENBORN. NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificity. NATURE COMMUNICATIONS. LONDON: NATURE PUBLISHING GROUP, 2013, vol. 4, May, p. "nestránkováno", 11 pp. ISSN 2041-1723. Available from: https://dx.doi.org/10.1038/ncomms2883. |
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@article{1166983,
author = {Byeon, InandJa L and Ahn, Jinwoo and Mitra, Mithun and Byeon, ChangandHyeock and Hercik, Kamil and Hritz, Jozef and Charlton, Lisa M and Levin, Judith G and Gronenborn, Angela M},
article_location = {LONDON},
article_number = {May},
doi = {http://dx.doi.org/10.1038/ncomms2883},
keywords = {single-stranded DNA; crystal structure; cytidine deaminase},
language = {eng},
issn = {2041-1723},
journal = {NATURE COMMUNICATIONS},
title = {NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificity},
volume = {4},
year = {2013}
}
TY - JOUR
ID - 1166983
AU - Byeon, In-Ja L - Ahn, Jinwoo - Mitra, Mithun - Byeon, Chang-Hyeock - Hercik, Kamil - Hritz, Jozef - Charlton, Lisa M - Levin, Judith G - Gronenborn, Angela M
PY - 2013
TI - NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificity
JF - NATURE COMMUNICATIONS
VL - 4
IS - May
SP - "nestránkováno"
EP - "nestránkováno"
PB - NATURE PUBLISHING GROUP
SN - 20411723
KW - single-stranded DNA
KW - crystal structure
KW - cytidine deaminase
N2 - Human APOBEC3A is a single-stranded DNA cytidine deaminase that restricts viral pathogens and endogenous retrotransposons, and has a role in the innate immune response. Furthermore, its potential to act as a genomic DNA mutator has implications for a role in carcinogenesis. A deeper understanding of APOBEC3A's deaminase and nucleic acid-binding properties, which is central to its biological activities, has been limited by the lack of structural information. Here we report the nuclear magnetic resonance solution structure of APOBEC3A and show that the critical interface for interaction with single-stranded DNA substrates includes residues extending beyond the catalytic centre. Importantly, by monitoring deaminase activity in real time, we find that A3A displays similar catalytic activity on APOBEC3A-specific TT (C) under barA- or A3G-specific CC (C) under barA-containing substrates, involving key determinants immediately 5' of the reactive C. Our results afford novel mechanistic insights into APOBEC3A-mediated deamination and provide the structural basis for further molecular studies.
ER -
BYEON, In-Ja L, Jinwoo AHN, Mithun MITRA, Chang-Hyeock BYEON, Kamil HERCIK, Jozef HRITZ, Lisa M CHARLTON, Judith G LEVIN and Angela M GRONENBORN. NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificity. \textit{NATURE COMMUNICATIONS}. LONDON: NATURE PUBLISHING GROUP, 2013, vol.~4, May, p.~''nestránkováno'', 11 pp. ISSN~2041-1723. Available from: https://dx.doi.org/10.1038/ncomms2883.
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