1z8y

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(New page: 200px<br /><applet load="1z8y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z8y" /> '''Mapping the E2 Glycoprotein of Alphaviruses'...)
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[[Image:1z8y.gif|left|200px]]<br /><applet load="1z8y" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1z8y.gif|left|200px]]<br /><applet load="1z8y" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1z8y" />
caption="1z8y" />
'''Mapping the E2 Glycoprotein of Alphaviruses'''<br />
'''Mapping the E2 Glycoprotein of Alphaviruses'''<br />
==Overview==
==Overview==
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The 9 A resolution cryo-electron microscopy map of Sindbis virus presented, here provides structural information on the polypeptide topology of the E2, protein, on the interactions between the E1 and E2 glycoproteins in the, formation of a heterodimer, on the difference in conformation of the two, types of trimeric spikes, on the interaction between the transmembrane, helices of the E1 and E2 proteins, and on the conformational changes that, occur when fusing with a host cell. The positions of various markers on, the E2 protein established the approximate topology of the E2 structure., The largest conformational differences between the icosahedral surface, spikes at icosahedral 3-fold and quasi-3-fold positions are associated, with the monomers closest to the 5-fold axes. The long E2 monomers, containing the cell receptor recognition motif at their extremities, are, shown to rotate by about 180 degrees and to move away from the center of, the spikes during fusion.
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The 9 A resolution cryo-electron microscopy map of Sindbis virus presented here provides structural information on the polypeptide topology of the E2 protein, on the interactions between the E1 and E2 glycoproteins in the formation of a heterodimer, on the difference in conformation of the two types of trimeric spikes, on the interaction between the transmembrane helices of the E1 and E2 proteins, and on the conformational changes that occur when fusing with a host cell. The positions of various markers on the E2 protein established the approximate topology of the E2 structure. The largest conformational differences between the icosahedral surface spikes at icosahedral 3-fold and quasi-3-fold positions are associated with the monomers closest to the 5-fold axes. The long E2 monomers, containing the cell receptor recognition motif at their extremities, are shown to rotate by about 180 degrees and to move away from the center of the spikes during fusion.
==About this Structure==
==About this Structure==
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1Z8Y is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sindbis_virus Sindbis virus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Z8Y OCA].
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1Z8Y is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sindbis_virus Sindbis virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z8Y OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Sindbis virus]]
[[Category: Sindbis virus]]
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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: Gabler, S.]]
[[Category: Gabler, S.]]
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[[Category: Kuhn, R.J.]]
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[[Category: Kuhn, R J.]]
[[Category: Mukhopadhyay, S.]]
[[Category: Mukhopadhyay, S.]]
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[[Category: Rossmann, M.G.]]
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[[Category: Rossmann, M G.]]
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[[Category: Strauss, E.G.]]
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[[Category: Strauss, E G.]]
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[[Category: Strauss, J.H.]]
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[[Category: Strauss, J H.]]
[[Category: Zhang, W.]]
[[Category: Zhang, W.]]
[[Category: cryo-electron microscopy]]
[[Category: cryo-electron microscopy]]
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[[Category: icosahedral virus]]
[[Category: icosahedral virus]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:18:35 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:13:13 2008''

Revision as of 14:13, 21 February 2008


1z8y

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Mapping the E2 Glycoprotein of Alphaviruses

Overview

The 9 A resolution cryo-electron microscopy map of Sindbis virus presented here provides structural information on the polypeptide topology of the E2 protein, on the interactions between the E1 and E2 glycoproteins in the formation of a heterodimer, on the difference in conformation of the two types of trimeric spikes, on the interaction between the transmembrane helices of the E1 and E2 proteins, and on the conformational changes that occur when fusing with a host cell. The positions of various markers on the E2 protein established the approximate topology of the E2 structure. The largest conformational differences between the icosahedral surface spikes at icosahedral 3-fold and quasi-3-fold positions are associated with the monomers closest to the 5-fold axes. The long E2 monomers, containing the cell receptor recognition motif at their extremities, are shown to rotate by about 180 degrees and to move away from the center of the spikes during fusion.

About this Structure

1Z8Y is a Protein complex structure of sequences from Sindbis virus. Full crystallographic information is available from OCA.

Reference

Mapping the structure and function of the E1 and E2 glycoproteins in alphaviruses., Mukhopadhyay S, Zhang W, Gabler S, Chipman PR, Strauss EG, Strauss JH, Baker TS, Kuhn RJ, Rossmann MG, Structure. 2006 Jan;14(1):63-73. PMID:16407066

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