1xak

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(New page: 200px<br /><applet load="1xak" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xak, resolution 1.80&Aring;" /> '''STRUCTURE OF THE SAR...)
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[[Image:1xak.jpg|left|200px]]<br /><applet load="1xak" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1xak, resolution 1.80&Aring;" />
caption="1xak, resolution 1.80&Aring;" />
'''STRUCTURE OF THE SARS-CORONAVIRUS ORF7A ACCESSORY PROTEIN'''<br />
'''STRUCTURE OF THE SARS-CORONAVIRUS ORF7A ACCESSORY PROTEIN'''<br />
==Overview==
==Overview==
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The open reading frame (ORF) 7a of the SARS-associated coronavirus, (SARS-CoV) encodes a unique type I transmembrane protein of unknown, function. We have determined the 1.8 A resolution crystal structure of the, N-terminal ectodomain of orf7a, revealing a compact seven-stranded beta, sandwich unexpectedly similar in fold and topology to members of the Ig, superfamily. We also demonstrate that, in SARS-CoV- infected cells, the, orf7a protein is expressed and retained intracellularly. Confocal, microscopy studies using orf7a and orf7a/CD4 chimeras implicate the short, cytoplasmic tail and transmembrane domain in trafficking of the protein, within the endoplasmic reticulum and Golgi network. Taken together, our, findings provide a structural and cellular framework in which to explore, the role of orf7a in SARS-CoV pathogenesis.
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The open reading frame (ORF) 7a of the SARS-associated coronavirus (SARS-CoV) encodes a unique type I transmembrane protein of unknown function. We have determined the 1.8 A resolution crystal structure of the N-terminal ectodomain of orf7a, revealing a compact seven-stranded beta sandwich unexpectedly similar in fold and topology to members of the Ig superfamily. We also demonstrate that, in SARS-CoV- infected cells, the orf7a protein is expressed and retained intracellularly. Confocal microscopy studies using orf7a and orf7a/CD4 chimeras implicate the short cytoplasmic tail and transmembrane domain in trafficking of the protein within the endoplasmic reticulum and Golgi network. Taken together, our findings provide a structural and cellular framework in which to explore the role of orf7a in SARS-CoV pathogenesis.
==About this Structure==
==About this Structure==
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1XAK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_sars_coronavirus Human sars coronavirus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XAK OCA].
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1XAK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_sars_coronavirus Human sars coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XAK OCA].
==Reference==
==Reference==
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[[Category: Human sars coronavirus]]
[[Category: Human sars coronavirus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Fremont, D.H.]]
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[[Category: Fremont, D H.]]
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[[Category: Lee, C.A.]]
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[[Category: Lee, C A.]]
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[[Category: MCSG, Midwest.Center.for.Structural.Genomics.]]
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[[Category: MCSG, Midwest Center for Structural Genomics.]]
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[[Category: Nelson, C.A.]]
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[[Category: Nelson, C A.]]
[[Category: beta sandwich]]
[[Category: beta sandwich]]
[[Category: i-set ig domain]]
[[Category: i-set ig domain]]
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[[Category: structural genomics]]
[[Category: structural genomics]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:56:48 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:52:46 2008''

Revision as of 13:52, 21 February 2008


1xak, resolution 1.80Å

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STRUCTURE OF THE SARS-CORONAVIRUS ORF7A ACCESSORY PROTEIN

Overview

The open reading frame (ORF) 7a of the SARS-associated coronavirus (SARS-CoV) encodes a unique type I transmembrane protein of unknown function. We have determined the 1.8 A resolution crystal structure of the N-terminal ectodomain of orf7a, revealing a compact seven-stranded beta sandwich unexpectedly similar in fold and topology to members of the Ig superfamily. We also demonstrate that, in SARS-CoV- infected cells, the orf7a protein is expressed and retained intracellularly. Confocal microscopy studies using orf7a and orf7a/CD4 chimeras implicate the short cytoplasmic tail and transmembrane domain in trafficking of the protein within the endoplasmic reticulum and Golgi network. Taken together, our findings provide a structural and cellular framework in which to explore the role of orf7a in SARS-CoV pathogenesis.

About this Structure

1XAK is a Single protein structure of sequence from Human sars coronavirus. Full crystallographic information is available from OCA.

Reference

Structure and intracellular targeting of the SARS-coronavirus Orf7a accessory protein., Nelson CA, Pekosz A, Lee CA, Diamond MS, Fremont DH, Structure. 2005 Jan;13(1):75-85. PMID:15642263

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