Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications

Lauren G. Holden, Courtney Prochnow, Y. Paul Chang, Ronda Bransteitter, Linda Chelico, Udayaditya Sen, Raymond C. Stevens, Myron F. Goodman and Xiaojiang S. Chen ()
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Lauren G. Holden: Molecular and Computational Biology, University of Southern California, Los Angeles, California 90089, USA
Courtney Prochnow: Molecular and Computational Biology, University of Southern California, Los Angeles, California 90089, USA
Y. Paul Chang: Molecular and Computational Biology, University of Southern California, Los Angeles, California 90089, USA
Ronda Bransteitter: Molecular and Computational Biology, University of Southern California, Los Angeles, California 90089, USA
Linda Chelico: Molecular and Computational Biology, University of Southern California, Los Angeles, California 90089, USA
Udayaditya Sen: Molecular and Computational Biology, University of Southern California, Los Angeles, California 90089, USA
Raymond C. Stevens: The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
Myron F. Goodman: Molecular and Computational Biology, University of Southern California, Los Angeles, California 90089, USA
Xiaojiang S. Chen: Molecular and Computational Biology, University of Southern California, Los Angeles, California 90089, USA

Nature, 2008, vol. 456, issue 7218, 121-124

Abstract: APOBEC proteins: deaminase domain structure This paper describes a high-resolution crystal structure of the catalytic deaminase CD2 domain of APOBEC3G, a human antiviral defence protein that restricts replication of HIV and hepatitis B virus. This structure will provide a basis to pursue further functional studies of proteins of the APOBEC superfamily that will facilitate our understanding of their important biological functions, such as how they interact with nucleic acid substrates for deamination, how their activity is regulated, and how they restrict HIV and other viral pathogens.

Date: 2008
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DOI: 10.1038/nature07357

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