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Solution Structure of a Bcl-2 Homolog from Kaposi Sarcoma Virus
Qiulong Huang, Andrew M. Petros, Herbert W. Virgin, Stephen W. Fesik and Edward T. Olejniczak
Proceedings of the National Academy of Sciences of the United States of America
Vol. 99, No. 6 (Mar. 19, 2002), pp. 3428-3433
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/3058143
Page Count: 6
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Kaposi sarcoma-associated herpes virus (KSHV) contains a gene that has functional and sequence homology to the apoptotic Bcl-2 family of proteins [Sarid, R., Sato, T., Bohenzky, R. A., Russo, J. J. & Chang, Y. (1997) Nat. Med. 3, 293-298]. The viral Bcl-2 protein promotes survival of infected cells and may contribute to the development of Kaposi sarcoma tumors [Boshoff, C. & Chang, Y. (2001) Annu. Rev. Med. 52, 453-470]. Here we describe the solution structure of the viral Bcl-2 homolog from KSHV. Comparison of the KSHV Bcl-2 structure to that of Bcl-2 and Bcl-xL shows that although the overall fold is the same, there are key differences in the lengths of the helices and loops. Binding studies on peptides derived from the Bcl-2 homology region 3 of proapoptotic family members indicate that the specificity of the viral protein is very different from what was previously observed for Bcl-xL and Bcl-2, suggesting that the viral protein has evolved to have a different mechanism of action than the host proteins.
Proceedings of the National Academy of Sciences of the United States of America © 2002 National Academy of Sciences