1vpn
From Proteopedia
(New page: 200px<br /><applet load="1vpn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vpn, resolution 2.0Å" /> '''UNASSEMBLED POLYOMAVI...) |
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| - | [[Image:1vpn.gif|left|200px]]<br /><applet load="1vpn" size=" | + | [[Image:1vpn.gif|left|200px]]<br /><applet load="1vpn" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1vpn, resolution 2.0Å" /> | caption="1vpn, resolution 2.0Å" /> | ||
'''UNASSEMBLED POLYOMAVIRUS VP1 PENTAMER'''<br /> | '''UNASSEMBLED POLYOMAVIRUS VP1 PENTAMER'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of a recombinant polyomavirus VP1 pentamer (residues | + | The crystal structure of a recombinant polyomavirus VP1 pentamer (residues 32-320) in complex with a branched disialylated hexasaccharide receptor fragment has been determined at 1.9 A resolution. The result extends our understanding of oligosaccharide receptor recognition. It also suggests a mechanism for enhancing the fidelity of virus assembly. We have previously described the structure of the complete polyomavirus particle complexed with this receptor fragment at 3.65 A. The model presented here offers a much more refined view of the interactions that determine carbohydrate recognition and allows us to assign additional specific contacts, in particular those involving the (alpha2,6)-linked, branching sialic acid. The structure of the unliganded VP1 pentamer, determined independently, shows that the oligosaccharide fits into a preformed groove and induces no measurable structural rearrangements. A comparison with assembled VP1 in the virus capsid reveals a rearrangement of residues 32-45 at the base of the pentamer. This segment may help prevent the formation of incorrectly assembled particles by reducing the likelihood that the C-terminal arm will fold back into its pentamer of origin. |
==About this Structure== | ==About this Structure== | ||
| - | 1VPN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Murine_polyomavirus Murine polyomavirus]. Full crystallographic information is available from [http:// | + | 1VPN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Murine_polyomavirus Murine polyomavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VPN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Murine polyomavirus]] | [[Category: Murine polyomavirus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Harrison, S | + | [[Category: Harrison, S C.]] |
[[Category: Stehle, T.]] | [[Category: Stehle, T.]] | ||
[[Category: virus assembly]] | [[Category: virus assembly]] | ||
[[Category: virus coat protein]] | [[Category: virus coat protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:37:16 2008'' |
Revision as of 13:37, 21 February 2008
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UNASSEMBLED POLYOMAVIRUS VP1 PENTAMER
Overview
The crystal structure of a recombinant polyomavirus VP1 pentamer (residues 32-320) in complex with a branched disialylated hexasaccharide receptor fragment has been determined at 1.9 A resolution. The result extends our understanding of oligosaccharide receptor recognition. It also suggests a mechanism for enhancing the fidelity of virus assembly. We have previously described the structure of the complete polyomavirus particle complexed with this receptor fragment at 3.65 A. The model presented here offers a much more refined view of the interactions that determine carbohydrate recognition and allows us to assign additional specific contacts, in particular those involving the (alpha2,6)-linked, branching sialic acid. The structure of the unliganded VP1 pentamer, determined independently, shows that the oligosaccharide fits into a preformed groove and induces no measurable structural rearrangements. A comparison with assembled VP1 in the virus capsid reveals a rearrangement of residues 32-45 at the base of the pentamer. This segment may help prevent the formation of incorrectly assembled particles by reducing the likelihood that the C-terminal arm will fold back into its pentamer of origin.
About this Structure
1VPN is a Single protein structure of sequence from Murine polyomavirus. Full crystallographic information is available from OCA.
Reference
High-resolution structure of a polyomavirus VP1-oligosaccharide complex: implications for assembly and receptor binding., Stehle T, Harrison SC, EMBO J. 1997 Aug 15;16(16):5139-48. PMID:9305654
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