Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2049585 | FEBS Letters | 2007 | 6 Pages |
Abstract
APOBEC3G is a single-strand DNA cytosine deaminase capable of blocking retrovirus and retrotransposon replication. APOBEC3G has two conserved zinc-coordinating motifs but only one is required for catalysis. Here, deletion analyses revealed that the minimal catalytic domain consists of residues 198-384. Size exclusion assays indicated that this protein is monomeric. Many (31/69) alanine substitution derivatives of APOBEC3G198-384 retained significant to full levels of activity. These data corroborated an APOBEC2-based structural model for the catalytic domain of APOBEC3G indicating that most non-essential residues are solvent accessible and most essential residues cluster within the protein core.
Keywords
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Kuan-Ming Chen, Natalia Martemyanova, Yongjian Lu, Keisuke Shindo, Hiroshi Matsuo, Reuben S. Harris,