Structure of the Uncleaved Ectodomain of the Paramyxovirus (HPIV3) Fusion Protein
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 conforma...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2005-06, Vol.102 (26), p.9288-9293 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Yin, Hsien-Sheng Paterson, Reay G. Wen, Xiaolin Lamb, Robert A. Jardetzky, Theodore S. |
| description | 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. |
| doi_str_mv | 10.1073/pnas.0503989102 |
| format | Article |
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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. 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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. 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| subjects | Animals Baculoviridae - metabolism Biological Sciences Cell Line Cloning, Molecular Crystal structure Crystallography, X-Ray Crystals Dimerization DNA, Complementary - metabolism Head Insecta Mechanical properties Membrane Fusion Microbiology Models, Molecular Molecular structure Monomers Mutation Paramyxovirinae - chemistry Protein Conformation Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Proteins Proteins - chemistry Recombinant Fusion Proteins - chemistry Trimers Viral fusion proteins Viral Fusion Proteins - chemistry Viral Fusion Proteins - metabolism Viral morphology Viral Proteins - chemistry Virology Viruses |
| title | Structure of the Uncleaved Ectodomain of the Paramyxovirus (HPIV3) Fusion Protein |
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