The latency associated nuclear antigen (LANA) protein of Kaposi's sarcoma associated herpesvirus (KSHV) plays several roles in KSHV latent infection including viral genome replication and segregation. Central to these roles is LANA's ability to self-associate and bind specific DNA sequences in the KSHV genome. The goal of this thesis was to characterize the LANA DNA binding and oligomerization domain. The C-terminal region of LANA (LANA-C), containing amino acids 941--1162, was cloned, expressed and purified and shown to possess sequence-specific DNA binding activity. DNA binding activity was further localized to the 1008--1162 amino acid fragment, while the 1021--1162 fragment had reduced DNA binding activity. For each of these LANA fragments, the addition of 0.5 M guanidine hydrochloride was found to greatly enhance purification. Each of the LANA fragments formed large oligmers, and gel filtration and glycerol gradient analyses of LANA-C indicated that the oligmeric state was an octamer.