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Article

Crystal Structure of a Soluble APOBEC3G Variant Suggests ssDNA to Bind in a Channel that Extends between the Two Domains.

Journal of molecular biology - 20 Nov 2020

Maiti Atanu, Myint Wazo, Delviks-Frankenberry Krista A, Hou Shurong, Kanai Tapan, Balachandran Vanivilasini, Sierra Rodriguez Christina, Tripathi Rashmi, Kurt Yilmaz Nese, Pathak Vinay K, Schiffer Celia A, Matsuo Hiroshi

Abstract excerpt

APOBEC3G (A3G) is a single-stranded DNA (ssDNA) cytosine deaminase that can restrict HIV-1 infection by mutating the viral genome. A3G consists of a non-catalytic N-terminal domain (NTD) and a catalytic C-terminal domain (CTD) connected by a short linker. While the CTD catalyzes cytosine deamination, the NTD is believed to provide additional affinity for ssDNA. Structures of both A3G domains have been solved...

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Identifiers

PMID: 33098858
DOI: 10.1016/j.jmb.2020.10.020
PMCID: PMC7771068

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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