1n6g

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(New page: 200px<br /><applet load="1n6g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n6g" /> '''The structure of immature Dengue-2 prM parti...)
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[[Image:1n6g.gif|left|200px]]<br /><applet load="1n6g" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1n6g.gif|left|200px]]<br /><applet load="1n6g" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1n6g" />
caption="1n6g" />
'''The structure of immature Dengue-2 prM particles'''<br />
'''The structure of immature Dengue-2 prM particles'''<br />
==Overview==
==Overview==
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Structures of prM-containing dengue and yellow fever virus particles were, determined to 16 and 25 A resolution, respectively, by cryoelectron, microscopy and image reconstruction techniques. The closely similar, structures show 60 icosahedrally organized trimeric spikes on the particle, surface. Each spike consists of three prM:E heterodimers, where E is an, envelope glycoprotein and prM is the precursor to the membrane protein M., The pre-peptide components of the prM proteins in each spike cover the, fusion peptides at the distal ends of the E glycoproteins in a manner, similar to the organization of the glycoproteins in the alphavirus spikes., Each heterodimer is associated with an E and a prM transmembrane density., These transmembrane densities represent either an EE or prMprM, antiparallel coiled coil by which each protein spans the membrane twice, leaving the C-terminus of each protein on the exterior of the viral, membrane, consistent with the predicted membrane-spanning domains of the, unprocessed polyprotein.
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Structures of prM-containing dengue and yellow fever virus particles were determined to 16 and 25 A resolution, respectively, by cryoelectron microscopy and image reconstruction techniques. The closely similar structures show 60 icosahedrally organized trimeric spikes on the particle surface. Each spike consists of three prM:E heterodimers, where E is an envelope glycoprotein and prM is the precursor to the membrane protein M. The pre-peptide components of the prM proteins in each spike cover the fusion peptides at the distal ends of the E glycoproteins in a manner similar to the organization of the glycoproteins in the alphavirus spikes. Each heterodimer is associated with an E and a prM transmembrane density. These transmembrane densities represent either an EE or prMprM antiparallel coiled coil by which each protein spans the membrane twice, leaving the C-terminus of each protein on the exterior of the viral membrane, consistent with the predicted membrane-spanning domains of the unprocessed polyprotein.
==About this Structure==
==About this Structure==
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1N6G 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N6G OCA].
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1N6G 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=1N6G OCA].
==Reference==
==Reference==
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[[Category: Dengue virus type 3]]
[[Category: Dengue virus type 3]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Baker, T.S.]]
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[[Category: Baker, T S.]]
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[[Category: Chipman, P.R.]]
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[[Category: Chipman, P R.]]
[[Category: Corver, J.]]
[[Category: Corver, J.]]
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[[Category: Kuhn, R.J.]]
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[[Category: Kuhn, R J.]]
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[[Category: Pletnev, S.V.]]
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[[Category: Pletnev, S V.]]
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[[Category: Rossmann, M.G.]]
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[[Category: Rossmann, M G.]]
[[Category: Sedlak, D.]]
[[Category: Sedlak, D.]]
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[[Category: Strauss, J.H.]]
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[[Category: Strauss, J H.]]
[[Category: Zhang, W.]]
[[Category: Zhang, W.]]
[[Category: Zhang, Y.]]
[[Category: Zhang, Y.]]
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[[Category: prm particle]]
[[Category: prm particle]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:00:13 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:02:44 2008''

Revision as of 12:02, 21 February 2008


1n6g

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The structure of immature Dengue-2 prM particles

Overview

Structures of prM-containing dengue and yellow fever virus particles were determined to 16 and 25 A resolution, respectively, by cryoelectron microscopy and image reconstruction techniques. The closely similar structures show 60 icosahedrally organized trimeric spikes on the particle surface. Each spike consists of three prM:E heterodimers, where E is an envelope glycoprotein and prM is the precursor to the membrane protein M. The pre-peptide components of the prM proteins in each spike cover the fusion peptides at the distal ends of the E glycoproteins in a manner similar to the organization of the glycoproteins in the alphavirus spikes. Each heterodimer is associated with an E and a prM transmembrane density. These transmembrane densities represent either an EE or prMprM antiparallel coiled coil by which each protein spans the membrane twice, leaving the C-terminus of each protein on the exterior of the viral membrane, consistent with the predicted membrane-spanning domains of the unprocessed polyprotein.

About this Structure

1N6G is a Single protein structure of sequence from Dengue virus type 3. Full crystallographic information is available from OCA.

Reference

Structures of immature flavivirus particles., Zhang Y, Corver J, Chipman PR, Zhang W, Pletnev SV, Sedlak D, Baker TS, Strauss JH, Kuhn RJ, Rossmann MG, EMBO J. 2003 Jun 2;22(11):2604-13. PMID:12773377

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