Understanding the structural basis of HIV-1 restriction by the full length double-domain APOBEC3G

Volume: 11, Issue: 1
Published: Jan 31, 2020
Abstract
APOBEC3G, a member of the double-domain cytidine deaminase (CD) APOBEC, binds RNA to package into virions and restrict HIV-1 through deamination-dependent or deamination-independent inhibition. Mainly due to lack of a full-length double-domain APOBEC structure, it is unknown how CD1/CD2 domains connect and how dimerization/multimerization is linked to RNA binding and virion packaging for HIV-1 restriction. We report rhesus macaque A3G structures...
Paper Details
Title
Understanding the structural basis of HIV-1 restriction by the full length double-domain APOBEC3G
Published Date
Jan 31, 2020
Volume
11
Issue
1
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