Kuan Ming Chen
Affiliation: University of Minnesota
- Extensive mutagenesis experiments corroborate a structural model for the DNA deaminase domain of APOBEC3GKuan Ming Chen
University of Minnesota, Department of Biochemistry, Molecular Biology and Biophysics, Minneapolis, MN 55455, United States
FEBS Lett 581:4761-6. 2007..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...
- Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3GKuan Ming Chen
Department of Biochemistry, Molecular Biology and Biophysics, of Minnesota, Minneapolis, Minnesota 55455, USA
Nature 452:116-9. 2008..The structure of the APOBEC3G catalytic domain will help us to understand functions of other family members and interactions that occur with pathogenic proteins such as HIV-1 Vif...
- Solution NMR structure of the N-terminal domain of the human DEK proteinMatthew Devany
Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455, USA
Protein Sci 17:205-15. 2008..Our study illustrates a new structural variant and reveals novel dsDNA-binding properties for proteins containing the SAP/SAF motif...
- Impact of H216 on the DNA binding and catalytic activities of the HIV restriction factor APOBEC3GStefan Harjes
Department of Biochemistry, Institute for Molecular Virology, University of Minnesota, Minneapolis, Minnesota, USA
J Virol 87:7008-14. 2013..Protonation of H216 appeared important for HIV-1 restriction activity as well, since substitutions of H216 resulted in lower restriction in vivo...
- An extended structure of the APOBEC3G catalytic domain suggests a unique holoenzyme modelElena Harjes
Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, 55455, USA
J Mol Biol 389:819-32. 2009....