| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 505652 | Computers in Biology and Medicine | 2009 | 7 Pages |
It is known that the EBNA-3 family proteins (EBNA-3, -4 and -6, alternative nomenclature EBNA-3A, B and C correspondingly) show a limited sequence similarity.We have analyzed EBNA-3 proteins both at the primary sequence and secondary structure levels. EBNA-3 and EBNA-4 were structurally more similar compared to other combinations with EBNA-6. We found “Stonin Homology Domain” profile in EBNA-4 and “Proline Rich Domain” in all EBNA-3 family of proteins. We have also found positive and negative charge clusters in all three proteins and mixed charge clusters in EBNA-3. Charged clusters are believed to play an important role in interactions with DNA or signaling proteins. Additionally, unique primary sequence repeats were found in all three proteins.
