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Structure of a human DNA repair protein UBA domain that interacts with HIV-1 Vpr
T Dieckmann1, E S Withers-Ward, M A Jarosinski
1Department of Chemistry and Biochemistry and the Molecular Biology Institute, University of California at Los Angeles, 90095, USA.
Abstract:
The HIV-1 protein Vpr is critical for a number of viral functions including a unique ability to arrest T-cells at a G2/M checkpoint and induce subsequent apoptosis. It has been shown to interact specifically with the second UBA (ubiquitin associated) domain found in the DNA repair protein HHR23A, a highly evolutionarily conserved protein. This domain is a commonly occurring sequence motif in some members of the ubiquitination pathway, UV excision repair proteins, and certain protein kinases. The three dimensional structure of the UBA domain, determined by NMR spectroscopy, is presented. The protein domain forms a compact three-helix bundle. One side of the protein has a hydrophobic surface that is the most likely Vpr target site.