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{{STRUCTURE_1g5g| PDB=1g5g | SCENE= }} | |||
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'''FRAGMENT OF FUSION PROTEIN FROM NEWCASTLE DISEASE VIRUS''' | '''FRAGMENT OF FUSION PROTEIN FROM NEWCASTLE DISEASE VIRUS''' | ||
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[[Category: Lawrence, M C.]] | [[Category: Lawrence, M C.]] | ||
[[Category: Smith, B J.]] | [[Category: Smith, B J.]] | ||
[[Category: | [[Category: Fusion protein]] | ||
[[Category: | [[Category: Ndv]] | ||
[[Category: | [[Category: Newcastle disease virus]] | ||
[[Category: | [[Category: Paramyxovirus]] | ||
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Revision as of 14:09, 2 May 2008
FRAGMENT OF FUSION PROTEIN FROM NEWCASTLE DISEASE VIRUS
Overview
BACKGROUND: Membrane fusion within the Paramyxoviridae family of viruses is mediated by a surface glycoprotein termed the "F", or fusion, protein. Membrane fusion is assumed to involve a series of structural transitions of F from a metastable (prefusion) state to a highly stable (postfusion) state. No detail is available at the atomic level regarding the metastable form of these proteins or regarding the transitions accompanying fusion. RESULTS: The three-dimensional structure of the fusion protein of Newcastle disease virus (NDV-F) has been determined. The trimeric NDV-F molecule is organized into head, neck, and stalk regions. The head is comprised of a highly twisted beta domain and an additional immunoglobulin-like beta domain. The neck is formed by the C-terminal extension of the heptad repeat region HR-A, capped by a four-helical bundle. The C terminus of HR-A is encased by a further helix HR-C and a 4-stranded beta sheet. The stalk is formed by the remaining visible portion of HR-A and by polypeptide immediately N-terminal to the C-terminal heptad repeat region HR-B. An axial channel extends through the head and neck and is fenestrated by three large radial channels located approximately at the head-neck interface. CONCLUSION: We propose that prior to fusion activation, the hydrophobic fusion peptides in NDV-F are sequestered within the radial channels within the head, with the central HR-A coiled coil being only partly formed. Fusion activation then involves, inter alia, the assembly of a complete HR-A coiled coil, with the fusion peptides and transmembrane anchors being brought into close proximity. The structure of NDV-F is fundamentally different than that of influenza virus hemagglutinin, in that the central coiled coil is in the opposite orientation with respect to the viral membrane.
About this Structure
1G5G is a Single protein structure of sequence from Newcastle disease virus. Full crystallographic information is available from OCA.
Reference
The structure of the fusion glycoprotein of Newcastle disease virus suggests a novel paradigm for the molecular mechanism of membrane fusion., Chen L, Gorman JJ, McKimm-Breschkin J, Lawrence LJ, Tulloch PA, Smith BJ, Colman PM, Lawrence MC, Structure. 2001 Mar 7;9(3):255-66. PMID:11286892 Page seeded by OCA on Fri May 2 17:09:38 2008
