1g5g
From Proteopedia
(New page: 200px<br /><applet load="1g5g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g5g, resolution 3.30Å" /> '''FRAGMENT OF FUSION P...) |
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| - | [[Image:1g5g.gif|left|200px]]<br /><applet load="1g5g" size=" | + | [[Image:1g5g.gif|left|200px]]<br /><applet load="1g5g" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1g5g, resolution 3.30Å" /> | caption="1g5g, resolution 3.30Å" /> | ||
'''FRAGMENT OF FUSION PROTEIN FROM NEWCASTLE DISEASE VIRUS'''<br /> | '''FRAGMENT OF FUSION PROTEIN FROM NEWCASTLE DISEASE VIRUS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: Membrane fusion within the Paramyxoviridae family of viruses | + | 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== | ==About this Structure== | ||
| - | 1G5G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Newcastle_disease_virus Newcastle disease virus] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1G5G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Newcastle_disease_virus Newcastle disease virus] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G5G OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Newcastle disease virus]] | [[Category: Newcastle disease virus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Lawrence, M | + | [[Category: Lawrence, M C.]] |
| - | [[Category: Smith, B | + | [[Category: Smith, B J.]] |
[[Category: NAG]] | [[Category: NAG]] | ||
[[Category: fusion protein]] | [[Category: fusion protein]] | ||
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[[Category: paramyxovirus]] | [[Category: paramyxovirus]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:46:18 2008'' |
Revision as of 10:46, 21 February 2008
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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 with as ligand. 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
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