1cn3
From Proteopedia
(New page: 200px<br /><applet load="1cn3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cn3, resolution 2.2Å" /> '''INTERACTION OF POLYOM...) |
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| - | [[Image:1cn3.gif|left|200px]]<br /><applet load="1cn3" size=" | + | [[Image:1cn3.gif|left|200px]]<br /><applet load="1cn3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cn3, resolution 2.2Å" /> | caption="1cn3, resolution 2.2Å" /> | ||
'''INTERACTION OF POLYOMAVIRUS INTERNAL PROTEIN VP2 WITH MAJOR CAPSID PROTEIN VP1 AND IMPLICATIONS FOR PARTICIPATION OF VP2 IN VIRAL ENTRY'''<br /> | '''INTERACTION OF POLYOMAVIRUS INTERNAL PROTEIN VP2 WITH MAJOR CAPSID PROTEIN VP1 AND IMPLICATIONS FOR PARTICIPATION OF VP2 IN VIRAL ENTRY'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A complex of the polyomavirus internal protein VP2/VP3 with the pentameric | + | A complex of the polyomavirus internal protein VP2/VP3 with the pentameric major capsid protein VP1 has been prepared by co-expression in Escherichia coli. A C-terminal segment of VP2/VP3 is required for tight association, and a crystal structure of this segment, complexed with a VP1 pentamer, has been determined at 2.2 A resolution. The structure shows specific contacts between a single copy of the internal protein and a pentamer of VP1. These interactions were not detected in the previously described structure of the virion, but the location of VP2 in the recombinant complex is consistent with features in the virion electron-density map. The C-terminus of VP2/VP3 inserts in an unusual, hairpin-like manner into the axial cavity of the VP1 pentamer, where it is anchored strongly by hydrophobic interactions. The remainder of the internal protein appears to have significant flexibility. This structure restricts possible models for exposure of the internal proteins during viral entry. |
==About this Structure== | ==About this Structure== | ||
| - | 1CN3 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Polyomavirus Polyomavirus]. Full crystallographic information is available from [http:// | + | 1CN3 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Polyomavirus Polyomavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CN3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Chen, X.]] | [[Category: Chen, X.]] | ||
| - | [[Category: Harrison, S | + | [[Category: Harrison, S C.]] |
[[Category: Stehle, T.]] | [[Category: Stehle, T.]] | ||
[[Category: viral coat protein vp1]] | [[Category: viral coat protein vp1]] | ||
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[[Category: viral entry]] | [[Category: viral entry]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:07:43 2008'' |
Revision as of 10:07, 21 February 2008
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INTERACTION OF POLYOMAVIRUS INTERNAL PROTEIN VP2 WITH MAJOR CAPSID PROTEIN VP1 AND IMPLICATIONS FOR PARTICIPATION OF VP2 IN VIRAL ENTRY
Overview
A complex of the polyomavirus internal protein VP2/VP3 with the pentameric major capsid protein VP1 has been prepared by co-expression in Escherichia coli. A C-terminal segment of VP2/VP3 is required for tight association, and a crystal structure of this segment, complexed with a VP1 pentamer, has been determined at 2.2 A resolution. The structure shows specific contacts between a single copy of the internal protein and a pentamer of VP1. These interactions were not detected in the previously described structure of the virion, but the location of VP2 in the recombinant complex is consistent with features in the virion electron-density map. The C-terminus of VP2/VP3 inserts in an unusual, hairpin-like manner into the axial cavity of the VP1 pentamer, where it is anchored strongly by hydrophobic interactions. The remainder of the internal protein appears to have significant flexibility. This structure restricts possible models for exposure of the internal proteins during viral entry.
About this Structure
1CN3 is a Protein complex structure of sequences from Polyomavirus. Full crystallographic information is available from OCA.
Reference
Interaction of polyomavirus internal protein VP2 with the major capsid protein VP1 and implications for participation of VP2 in viral entry., Chen XS, Stehle T, Harrison SC, EMBO J. 1998 Jun 15;17(12):3233-40. PMID:9628860
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