The Kylie Walters lab (Xiang Chen, Leah Randles, Naixia Zhang) with collaborators have described a new substrate receptor in the proteasome in two Nature May 22nd manuscripts. This work considerably advances our understanding of how
the main agent of protein destruction catches its targets.

Hiroshi Matsuo, and Reuben Harris have determined the structure of APOBEC3G—a protein that inhibits the AIDS virus, HIV. This discovery is the first to shed light on the atomic structure of the protein. It will help researchers manipulate APOBEC3G to make it effective in combating HIV. The research was released on the Nature advance online publication - February 20, 2008.


The human APOBEC3G protein is a single-stranded DNA (ssDNA) cytosine deaminase that can inhibit retrovirus infections by converting viral DNA cytosines to uracils, effectively mutagenizing viral genomes. This protein is additionally remarkable because it can inhibit the AIDS virus HIV-1. We have determined the three dimensional structure of the deaminase domain of APOBEC3G using NMR spectroscopy. This molecular structure is the first for any member of this important class of vertebrate enzymes. The Figure shows the surface of the APOBEC3G protein, including arginine (R) amino acids that are involved in binding ssDNA.