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Structure of the catalytically active APOBEC3G bound to a DNA oligonucleotide inhibitor reveals tetrahedral geometry of the transition state

Authors :
Atanu Maiti
Adam K. Hedger
Wazo Myint
Vanivilasini Balachandran
Jonathan K. Watts
Celia A. Schiffer
Hiroshi Matsuo
Source :
Nature Communications, Vol 13, Iss 1, Pp 1-10 (2022)
Publication Year :
2022
Publisher :
Nature Portfolio, 2022.

Abstract

Here, the enzymatic activity of APOBEC3G resulting in conversion of 2′-deoxy-zebularine into a hydration product allowed the authors to capture the transition state, which provides a blueprint for designing a new class of transition state-mimicking inhibitors for this class of enzyme.

Subjects

Subjects :
Science

Details

Language :
English
ISSN :
20411723
Volume :
13
Issue :
1
Database :
Directory of Open Access Journals
Journal :
Nature Communications
Publication Type :
Academic Journal
Accession number :
edsdoj.9b59b40269cb4ef4b61dc593fa6d83f7
Document Type :
article
Full Text :
https://doi.org/10.1038/s41467-022-34752-1