Comparative analysis of the Epstein-Barr virus encoded nuclear proteins of EBNA-3 family.
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.
Yenamandra
Surya Pavan
SP
Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet, S-17177 Stockholm, Sweden.
Sompallae
Ramakrishna
R
Klein
George
G
Kashuba
Elena
E
D000595:Amino Acid Sequence; D004854:Herpesvirus 4, Human / Q000737:chemistry*; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D014764:Viral Proteins / Q000737:chemistry*
D014764:Viral Proteins