1wyy
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(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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Revision as of 03:38, 21 November 2007
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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 CL 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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