1d4m
From Proteopedia
(New page: 200px<br /><applet load="1d4m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d4m, resolution 2.9Å" /> '''THE CRYSTAL STRUCTURE...) |
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| - | [[Image:1d4m.gif|left|200px]]<br /><applet load="1d4m" size=" | + | [[Image:1d4m.gif|left|200px]]<br /><applet load="1d4m" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1d4m, resolution 2.9Å" /> | caption="1d4m, resolution 2.9Å" /> | ||
'''THE CRYSTAL STRUCTURE OF COXSACKIEVIRUS A9 TO 2.9 A RESOLUTION'''<br /> | '''THE CRYSTAL STRUCTURE OF COXSACKIEVIRUS A9 TO 2.9 A RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: Coxsackievirus A9 (CAV9), a human pathogen causing symptoms | + | BACKGROUND: Coxsackievirus A9 (CAV9), a human pathogen causing symptoms ranging from common colds to fatal infections of the central nervous system, is an icosahedral single-stranded RNA virus that belongs to the genus Enterovirus of the family Picornaviridae. One of the four capsid proteins, VP1, includes the arginine-glycine-aspartate (RGD) motif within its C-terminal extension. This region binds to integrin alpha v beta 3, the only receptor for CAV9 to be conclusively identified to date. RESULTS: The crystal structure of CAV9 in complex with the antiviral compound WIN 51711 has been solved to 2.9 A resolution. The structures of the four capsid proteins, VP1 to VP4, resemble those of other picornaviruses. The antiviral compound is bound in the VP1 hydrophobic pocket, and it is possible that the pocket entrance contains a second WIN 51711 molecule. Continuous electron density for the VP1 N terminus provides a complete picture of the structure close to the fivefold axis. The VP1 C-terminal portion is on the outer surface of the virus and becomes disordered five-residues N-terminal to the RGD motif. CONCLUSIONS: The RGD motif is exposed and flexible in common with other known integrin ligands. Although CAV9 resembles coxsackie B viruses (CBVs), several substitutions in the areas implicated in CBV receptor attachment suggest it may recognise a different receptor. The structure along the fivefold axis provides new information on the uncoating mechanism of enteroviruses. CAV9 might bind a larger natural pocket factor than other picornaviruses, an observation of particular relevance to the design of new antiviral compounds. |
==About this Structure== | ==About this Structure== | ||
| - | 1D4M is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_coxsackievirus_a21 Human coxsackievirus a21] with MYR and W71 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1D4M is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_coxsackievirus_a21 Human coxsackievirus a21] with <scene name='pdbligand=MYR:'>MYR</scene> and <scene name='pdbligand=W71:'>W71</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D4M OCA]. |
==Reference== | ==Reference== | ||
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[[Category: win compound]] | [[Category: win compound]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:12:54 2008'' |
Revision as of 10:12, 21 February 2008
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THE CRYSTAL STRUCTURE OF COXSACKIEVIRUS A9 TO 2.9 A RESOLUTION
Overview
BACKGROUND: Coxsackievirus A9 (CAV9), a human pathogen causing symptoms ranging from common colds to fatal infections of the central nervous system, is an icosahedral single-stranded RNA virus that belongs to the genus Enterovirus of the family Picornaviridae. One of the four capsid proteins, VP1, includes the arginine-glycine-aspartate (RGD) motif within its C-terminal extension. This region binds to integrin alpha v beta 3, the only receptor for CAV9 to be conclusively identified to date. RESULTS: The crystal structure of CAV9 in complex with the antiviral compound WIN 51711 has been solved to 2.9 A resolution. The structures of the four capsid proteins, VP1 to VP4, resemble those of other picornaviruses. The antiviral compound is bound in the VP1 hydrophobic pocket, and it is possible that the pocket entrance contains a second WIN 51711 molecule. Continuous electron density for the VP1 N terminus provides a complete picture of the structure close to the fivefold axis. The VP1 C-terminal portion is on the outer surface of the virus and becomes disordered five-residues N-terminal to the RGD motif. CONCLUSIONS: The RGD motif is exposed and flexible in common with other known integrin ligands. Although CAV9 resembles coxsackie B viruses (CBVs), several substitutions in the areas implicated in CBV receptor attachment suggest it may recognise a different receptor. The structure along the fivefold axis provides new information on the uncoating mechanism of enteroviruses. CAV9 might bind a larger natural pocket factor than other picornaviruses, an observation of particular relevance to the design of new antiviral compounds.
About this Structure
1D4M is a Protein complex structure of sequences from Human coxsackievirus a21 with and as ligands. Full crystallographic information is available from OCA.
Reference
The crystal structure of coxsackievirus A9: new insights into the uncoating mechanisms of enteroviruses., Hendry E, Hatanaka H, Fry E, Smyth M, Tate J, Stanway G, Santti J, Maaronen M, Hyypia T, Stuart D, Structure. 1999 Dec 15;7(12):1527-38. PMID:10647183
Page seeded by OCA on Thu Feb 21 12:12:54 2008
Categories: Human coxsackievirus a21 | Protein complex | Fry, E. | Hatanaka, H. | Hendry, E. | Hyypia, T. | Maaronen, M. | Santti, J. | Smyth, M. | Stanway, G. | Stuart, D. | Tate, J. | MYR | W71 | Icosahedral virus | Picornavirus structure | Rgd | Uncoating | Virus-receptor interaction | Virus/viral protein | Win compound
