Structure of the uncleaved ectodomain of the paramyxovirus (hPIV3) fusion protein

Proceedings of the National Academy of Sciences of the United States of America - Tập 102 Số 26 - Trang 9288-9293 - 2005
Hsien-Sheng Yin1, Reay G. Paterson1, Xiaolin Wen1, Robert A. Lamb1, Theodore S. Jardetzky1
1Department of Biochemistry, Molecular Biology, and Cell Biology, Howard Hughes Medical Institute, Northwestern University, Evanston, IL 60208-3500

Tóm tắt

Class I viral fusion proteins share common mechanistic and structural features but little sequence similarity. Structural insights into the protein conformational changes associated with membrane fusion are based largely on studies of the influenza virus hemagglutinin in pre- and postfusion conformations. Here, we present the crystal structure of the secreted, uncleaved ectodomain of the paramyxovirus, human parainfluenza virus 3 fusion (F) protein, a member of the class I viral fusion protein group. The secreted human parainfluenza virus 3 F forms a trimer with distinct head, neck, and stalk regions. Unexpectedly, the structure reveals a six-helix bundle associated with the postfusion form of F, suggesting that the anchor-minus ectodomain adopts a conformation largely similar to the postfusion state. The transmembrane anchor domains of F may therefore profoundly influence the folding energetics that establish and maintain a metastable, prefusion state.

Từ khóa


Tài liệu tham khảo

10.1023/A:1010467106305

10.1038/427307a

Lamb R. A. & Kolakofsky D. (2001) in Fields Virology eds. Knipe D. M. & Howley P. M. (Lippincott Williams & Wilkins Philadelphia) 4th Ed. pp. 1305-1340.

Earp, L. J., Delos, S. E., Park, H. E. & White, J. M. (2005) Curr. Top. Microbiol. Immunol. 285, 25-66.15609500

10.1146/annurev.biochem.69.1.531

10.1038/nrm1076

10.1016/S0065-3233(03)01009-X

10.1146/annurev.biochem.70.1.777

10.1093/emboj/20.15.4024

10.1083/jcb.151.2.413

10.1038/289366a0

10.1016/S0092-8674(00)81771-7

10.1038/371037a0

10.1073/pnas.96.16.8967

10.1016/S1097-2765(00)80458-X

10.1073/pnas.260499197

10.1016/S0969-2126(01)00581-0

10.1107/S0907444994003112

10.1107/S0907444903028956

10.1107/S0907444998003254

10.1107/S0108767390010224

10.1107/S0021889892009944

10.1006/viro.2001.1172

10.1038/nsb0596-465

10.1093/emboj/cdg385

10.1006/viro.1998.9242

10.1006/viro.1998.9532

10.1083/jcb.200305130

10.1006/viro.2000.0267

10.1128/JVI.78.24.13727-13742.2004

10.1099/0022-1317-71-5-1189

10.1006/viro.2002.1497

10.1099/vir.0.80318-0

10.1073/pnas.0403339101

10.1128/JVI.75.19.8999-9009.2001

10.1002/j.1460-2075.1990.tb08155.x

10.1073/pnas.92.26.12205

10.1021/bi049807k

Thông tin
Thông tin xuất bản

Proceedings of the National Academy of Sciences of the United States of America

Tập 102 Số 26

9288-9293

Thông tin tác giả