NMR assignments and the identification of the secondary structure of the anti-retroviral cytidine deaminase.
APOBEC3G (apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3G) is known to have a role in intrinsic cellular immunity against human immunodeficiency virus type1 (HIV-1). The antiretroviral activity of APOBEC3G (APO3G) is associated with the hypermutation of viral DNA through cytidine deamination. APO3G contains two cytidine deaminase domains that are characterised by highly conserved zinc-coordinating motif. It is known that only the C-terminal domain of APO3G (c-APO3G) has the catalytic activity. To shed light on the molecular mechanism of action by which APO3G inactivates HIV-1, we have undertaken the structural and binding studies by NMR. Here, we show the achievement of backbone assignments of c-APO3G and the identification of the secondary structure deduced from chemical shift index (CSI) and NOE data.
Furukawa
Ayako
A
Supramolecular Biology, International Graduate School of Arts and Sciences, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan.
Nagata
Takashi
T
Habu
Yuichirou
Y
Sugiyama
Ryuichi
R
Hayashi
Fumiaki
F
Yokoyama
Shigeyuki
S
Takaku
Hiroshi
H
Katahira
Masato
M
D000071480:APOBEC-3G Deaminase; D003564:Cytidine Deaminase / Q000737:chemistry*; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D040681:Structural Homology, Protein
D000071480:APOBEC-3G Deaminase; C464924:APOBEC3G protein, human; D003564:Cytidine Deaminase