Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 281, Issue 50, Pages 38122-38126Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.C600253200
Keywords
-
Categories
Funding
- NCRR NIH HHS [P41 RR001646, RR 01646] Funding Source: Medline
- NIAID NIH HHS [T32 AI 49815, R21 AI058789, T32 AI049815] Funding Source: Medline
- NIGMS NIH HHS [DMR0225180] Funding Source: Medline
Ask authors/readers for more resources
Human APOBEC3G ( hA3G) is a cytidine deaminase that restricts human immunodeficiency virus (HIV)-1 infection in a vif ( the virion infectivity factor from HIV)-dependent manner. hA3G from HIV-permissive activated CD4+ T-cells exists as an inactive, high molecular mass (HMM) complex that can be transformed in vitro into an active, low molecular mass (LMM) variant comparable with that of HIV-non-permissive CD4+ T-cells. Here we present low resolution structures of hA3G in HMM and LMM forms determined by small angle x-ray scattering and advanced shape reconstruction methods. The results show that LMM particles have an extended shape, dissimilar to known cytidine deaminases, featuring novel tail-to-tail dimerization. Shape analysis of LMM and HMM structures revealed how symmetric association of dimers could lead to minimal HMM variants. These observations imply that the disruption of cellular HMM particles may require regulation of protein-RNA, as well as protein-protein interactions, which has implications for therapeutic development.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available