1r6r
From Proteopedia
(New page: 200px<br /><applet load="1r6r" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r6r" /> '''Solution Structure of Dengue Virus Capsid Pr...) |
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'''Solution Structure of Dengue Virus Capsid Protein Reveals a New Fold'''<br /> | '''Solution Structure of Dengue Virus Capsid Protein Reveals a New Fold'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Dengue virus is responsible for approximately 50-100 million infections, resulting in nearly 24,000 deaths annually. The capsid (C) protein of | + | Dengue virus is responsible for approximately 50-100 million infections, resulting in nearly 24,000 deaths annually. The capsid (C) protein of dengue virus is essential for specific encapsidation of the RNA genome, but little structural information on the C protein is available. We report the solution structure of the 200-residue homodimer of dengue 2 C protein. The structure provides, to our knowledge, the first 3D picture of a flavivirus C protein and identifies a fold that includes a large dimerization surface contributed by two pairs of helices, one of which has characteristics of a coiled-coil. NMR structure determination involved a secondary structure sorting approach to facilitate assignment of the intersubunit nuclear Overhauser effect interactions. The dimer of dengue C protein has an unusually high net charge, and the structure reveals an asymmetric distribution of basic residues over the surface of the protein. Nearly half of the basic residues lie along one face of the dimer. In contrast, the conserved hydrophobic region forms an extensive apolar surface at a dimer interface on the opposite side of the molecule. We propose a model for the interaction of dengue C protein with RNA and the viral membrane that is based on the asymmetric charge distribution of the protein and is consistent with previously reported results. |
==About this Structure== | ==About this Structure== | ||
| - | 1R6R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dengue_virus_type_3 Dengue virus type 3]. Full crystallographic information is available from [http:// | + | 1R6R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dengue_virus_type_3 Dengue virus type 3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R6R OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Dengue virus type 3]] | [[Category: Dengue virus type 3]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Groesch, T | + | [[Category: Groesch, T D.]] |
| - | [[Category: Jones, C | + | [[Category: Jones, C T.]] |
| - | [[Category: Kuhn, R | + | [[Category: Kuhn, R J.]] |
[[Category: Ma, L.]] | [[Category: Ma, L.]] | ||
| - | [[Category: Post, C | + | [[Category: Post, C B.]] |
[[Category: alpha helical]] | [[Category: alpha helical]] | ||
[[Category: dimer]] | [[Category: dimer]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:47:47 2008'' |
Revision as of 12:47, 21 February 2008
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Solution Structure of Dengue Virus Capsid Protein Reveals a New Fold
Overview
Dengue virus is responsible for approximately 50-100 million infections, resulting in nearly 24,000 deaths annually. The capsid (C) protein of dengue virus is essential for specific encapsidation of the RNA genome, but little structural information on the C protein is available. We report the solution structure of the 200-residue homodimer of dengue 2 C protein. The structure provides, to our knowledge, the first 3D picture of a flavivirus C protein and identifies a fold that includes a large dimerization surface contributed by two pairs of helices, one of which has characteristics of a coiled-coil. NMR structure determination involved a secondary structure sorting approach to facilitate assignment of the intersubunit nuclear Overhauser effect interactions. The dimer of dengue C protein has an unusually high net charge, and the structure reveals an asymmetric distribution of basic residues over the surface of the protein. Nearly half of the basic residues lie along one face of the dimer. In contrast, the conserved hydrophobic region forms an extensive apolar surface at a dimer interface on the opposite side of the molecule. We propose a model for the interaction of dengue C protein with RNA and the viral membrane that is based on the asymmetric charge distribution of the protein and is consistent with previously reported results.
About this Structure
1R6R is a Single protein structure of sequence from Dengue virus type 3. Full crystallographic information is available from OCA.
Reference
Solution structure of dengue virus capsid protein reveals another fold., Ma L, Jones CT, Groesch TD, Kuhn RJ, Post CB, Proc Natl Acad Sci U S A. 2004 Mar 9;101(10):3414-9. Epub 2004 Mar 1. PMID:14993605
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