|
|
| Line 1: |
Line 1: |
| [[Image:1g5g.gif|left|200px]] | | {{Seed}} |
| | [[Image:1g5g.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
| Line 9: |
Line 10: |
| {{STRUCTURE_1g5g| PDB=1g5g | SCENE= }} | | {{STRUCTURE_1g5g| PDB=1g5g | SCENE= }} |
|
| |
|
| '''FRAGMENT OF FUSION PROTEIN FROM NEWCASTLE DISEASE VIRUS'''
| | ===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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11286892}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11286892 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_11286892}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
| Line 28: |
Line 32: |
| [[Category: Newcastle disease virus]] | | [[Category: Newcastle disease virus]] |
| [[Category: Paramyxovirus]] | | [[Category: Paramyxovirus]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:09:38 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:27:58 2008'' |
