Comparative analysis of the Epstein-Barr virus encoded nuclear proteins of EBNA-3 family |
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Authors: | Surya Pavan Yenamandra Ramakrishna Sompallae Elena Kashuba |
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Affiliation: | a Department of Microbiology, Tumor and Cell Biology (MTC), Karolinska Institutet, Box 280, S-17177 Stockholm, Sweden b IRIS (Center for Integrative Recognition in the Immune System), Karolinska Institutet, S-17177 Stockholm, Sweden c Department of Cellular and Molecular Biology (CMB), Karolinska Institutet, Box 280, S-17177 Stockholm, Sweden |
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Abstract: | 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. |
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Keywords: | EBNA3 family proteins Secondary structure analysis Stonin homology domain Praline rich domain Charge clusters |
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