1uzg
From Proteopedia
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| - | [[Image:1uzg.gif|left|200px]]<br /><applet load="1uzg" size=" | + | [[Image:1uzg.gif|left|200px]]<br /><applet load="1uzg" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1uzg, resolution 3.50Å" /> | caption="1uzg, resolution 3.50Å" /> | ||
'''CRYSTAL STRUCTURE OF THE DENGUE TYPE 3 VIRUS ENVELOPE PROTEIN'''<br /> | '''CRYSTAL STRUCTURE OF THE DENGUE TYPE 3 VIRUS ENVELOPE PROTEIN'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1UZG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dengue_virus_type_1 Dengue virus type 1] with FUL, BMA and NAG as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Mutation At This Position Causes Escape From Neutralizat ...'>AC1</scene>. Full crystallographic information is available from [http:// | + | 1UZG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dengue_virus_type_1 Dengue virus type 1] with <scene name='pdbligand=FUL:'>FUL</scene>, <scene name='pdbligand=BMA:'>BMA</scene> and <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Mutation+At+This+Position+Causes+Escape+From+Neutralizat+...'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UZG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: virus/viral protein]] | [[Category: virus/viral protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:13:00 2008'' |
Revision as of 08:13, 3 February 2008
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CRYSTAL STRUCTURE OF THE DENGUE TYPE 3 VIRUS ENVELOPE PROTEIN
Overview
Dengue virus is an emerging global health threat. The major envelope, glycoprotein, E, mediates viral attachment and entry by membrane fusion., Antibodies that bind but fail to neutralize noncognate serotypes enhance, infection. We have determined the crystal structure of a soluble fragment, of the envelope glycoprotein E from dengue virus type 3. The structure, closely resembles those of E proteins from dengue type 2 and tick-borne, encephalitis viruses. Serotype-specific neutralization escape mutants in, dengue virus E proteins are all located on a surface of domain III, which, has been implicated in receptor binding. While antibodies against epitopes, in domain I are nonneutralizing in dengue virus, there are neutralizing, antibodies that recognize serotype-conserved epitopes in domain II. The, mechanism of neutralization for these antibodies is probably inhibition of, membrane fusion. Our structure shows that neighboring glycans on the viral, surface are spaced widely enough (at least 32 A) that they can interact, with multiple carbohydrate recognition domains on oligomeric lectins such, as DC-SIGN, ensuring maximum affinity for these putative receptors.
About this Structure
1UZG is a Single protein structure of sequence from Dengue virus type 1 with , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein., Modis Y, Ogata S, Clements D, Harrison SC, J Virol. 2005 Jan;79(2):1223-31. PMID:15613349
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Categories: Dengue virus type 1 | Single protein | Harrison, S.C. | Modis, Y. | BMA | FUL | NAG | Atp-binding | Class 2 fusion protein | Dengue virus | Envelope protein | Flavivirus | Fusion loop | Glycoprotein | Helicase | Hydrolase | Membrane fusion | Nonstructural protein | Polyprotein | Rna-directed rna polymerase | Transferase | Transmembrane | Virus/viral protein
