1wyy
From Proteopedia
(New page: 200px<br /><applet load="1wyy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wyy, resolution 2.2Å" /> '''Post-fusion hairpin c...) |
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| - | [[Image:1wyy.gif|left|200px]]<br /><applet load="1wyy" size=" | + | [[Image:1wyy.gif|left|200px]]<br /><applet load="1wyy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wyy, resolution 2.2Å" /> | caption="1wyy, resolution 2.2Å" /> | ||
'''Post-fusion hairpin conformation of the sars coronavirus spike glycoprotein'''<br /> | '''Post-fusion hairpin conformation of the sars coronavirus spike glycoprotein'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The coronavirus spike glycoprotein is a class I membrane fusion protein | + | The coronavirus spike glycoprotein is a class I membrane fusion protein with two characteristic heptad repeat regions (HR1 and HR2) in its ectodomain. Here, we report the X-ray structure of a previously characterized HR1/HR2 complex of the severe acute respiratory syndrome coronavirus spike protein. As expected, the HR1 and HR2 segments are organized in antiparallel orientations within a rod-like molecule. The HR1 helices form an exceptionally long (120 A) internal coiled coil stabilized by hydrophobic and polar interactions. A striking arrangement of conserved asparagine and glutamine residues of HR1 propagates from two central chloride ions, providing hydrogen-bonding "zippers" that strongly constrain the path of the HR2 main chain, forcing it to adopt an extended conformation at either end of a short HR2 alpha-helix. |
==About this Structure== | ==About this Structure== | ||
| - | 1WYY 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] with CL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1WYY 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] with <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WYY OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Human sars coronavirus]] | [[Category: Human sars coronavirus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bosch, B | + | [[Category: Bosch, B J.]] |
[[Category: Duquerroy, S.]] | [[Category: Duquerroy, S.]] | ||
| - | [[Category: Rey, F | + | [[Category: Rey, F A.]] |
| - | [[Category: Rottier, P | + | [[Category: Rottier, P J.M.]] |
[[Category: Vigouroux, A.]] | [[Category: Vigouroux, A.]] | ||
[[Category: CL]] | [[Category: CL]] | ||
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[[Category: viral protein]] | [[Category: viral protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:49:34 2008'' |
Revision as of 13:49, 21 February 2008
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Post-fusion hairpin conformation of the sars coronavirus spike glycoprotein
Overview
The coronavirus spike glycoprotein is a class I membrane fusion protein with two characteristic heptad repeat regions (HR1 and HR2) in its ectodomain. Here, we report the X-ray structure of a previously characterized HR1/HR2 complex of the severe acute respiratory syndrome coronavirus spike protein. As expected, the HR1 and HR2 segments are organized in antiparallel orientations within a rod-like molecule. The HR1 helices form an exceptionally long (120 A) internal coiled coil stabilized by hydrophobic and polar interactions. A striking arrangement of conserved asparagine and glutamine residues of HR1 propagates from two central chloride ions, providing hydrogen-bonding "zippers" that strongly constrain the path of the HR2 main chain, forcing it to adopt an extended conformation at either end of a short HR2 alpha-helix.
About this Structure
1WYY is a Single protein structure of sequence from Human sars coronavirus with as ligand. Full crystallographic information is available from OCA.
Reference
Central ions and lateral asparagine/glutamine zippers stabilize the post-fusion hairpin conformation of the SARS coronavirus spike glycoprotein., Duquerroy S, Vigouroux A, Rottier PJ, Rey FA, Bosch BJ, Virology. 2005 May 10;335(2):276-85. PMID:15840526
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