2beq
From Proteopedia
(New page: 200px<br /><applet load="2beq" size="450" color="white" frame="true" align="right" spinBox="true" caption="2beq, resolution 1.60Å" /> '''STRUCTURE OF A PROTE...) |
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| - | [[Image:2beq.gif|left|200px]]<br /><applet load="2beq" size=" | + | [[Image:2beq.gif|left|200px]]<br /><applet load="2beq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2beq, resolution 1.60Å" /> | caption="2beq, resolution 1.60Å" /> | ||
'''STRUCTURE OF A PROTEOLYTICALLY RESISTANT CORE FROM THE SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS S2 FUSION PROTEIN'''<br /> | '''STRUCTURE OF A PROTEOLYTICALLY RESISTANT CORE FROM THE SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS S2 FUSION PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A coronavirus (CoV) has recently been identified as the causative agent of | + | A coronavirus (CoV) has recently been identified as the causative agent of the severe acute respiratory syndrome (SARS) in humans. CoVs enter target cells through fusion of viral and cellular membranes mediated by the viral envelope glycoprotein S. We have determined by x-ray crystallography the structure of a proteolytically stable core fragment from the heptad repeat (HR) regions HR1 and HR2 of the SARS-CoV S protein. We have also determined the structure of an HR1-HR2 S core fragment, containing a shorter HR1 peptide and a C-terminally longer HR2 peptide that extends up to the transmembrane region. In these structures, three HR1 helices form a parallel coiled-coil trimer, whereas three HR2 peptides pack in an oblique and antiparallel fashion into the coiled-coil hydrophobic grooves, adopting mixed extended and alpha-helical conformations as in postfusion paramyxoviruses F proteins structures. Our structure positions a previously proposed internal fusion peptide adjacent to the N-terminus of HR1. Peptides from the HR2 region of SARS-CoV S have been shown to inhibit viral entry and infection in vitro. The structures presented here can thus open the path to the design of small-molecule inhibitors of viral entry and candidate vaccine antigens against this virus. |
==About this Structure== | ==About this Structure== | ||
| - | 2BEQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with NH2 and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2BEQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=NH2:'>NH2</scene> and <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BEQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ingallinella, P.]] | [[Category: Ingallinella, P.]] | ||
[[Category: Pessi, A.]] | [[Category: Pessi, A.]] | ||
| - | [[Category: Supekar, V | + | [[Category: Supekar, V M.]] |
[[Category: ACE]] | [[Category: ACE]] | ||
[[Category: NH2]] | [[Category: NH2]] | ||
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[[Category: virulence]] | [[Category: virulence]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:37:00 2008'' |
Revision as of 14:37, 21 February 2008
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STRUCTURE OF A PROTEOLYTICALLY RESISTANT CORE FROM THE SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS S2 FUSION PROTEIN
Overview
A coronavirus (CoV) has recently been identified as the causative agent of the severe acute respiratory syndrome (SARS) in humans. CoVs enter target cells through fusion of viral and cellular membranes mediated by the viral envelope glycoprotein S. We have determined by x-ray crystallography the structure of a proteolytically stable core fragment from the heptad repeat (HR) regions HR1 and HR2 of the SARS-CoV S protein. We have also determined the structure of an HR1-HR2 S core fragment, containing a shorter HR1 peptide and a C-terminally longer HR2 peptide that extends up to the transmembrane region. In these structures, three HR1 helices form a parallel coiled-coil trimer, whereas three HR2 peptides pack in an oblique and antiparallel fashion into the coiled-coil hydrophobic grooves, adopting mixed extended and alpha-helical conformations as in postfusion paramyxoviruses F proteins structures. Our structure positions a previously proposed internal fusion peptide adjacent to the N-terminus of HR1. Peptides from the HR2 region of SARS-CoV S have been shown to inhibit viral entry and infection in vitro. The structures presented here can thus open the path to the design of small-molecule inhibitors of viral entry and candidate vaccine antigens against this virus.
About this Structure
2BEQ is a Protein complex structure of sequences from [1] with and as ligands. Full crystallographic information is available from OCA.
Reference
Structure of a proteolytically resistant core from the severe acute respiratory syndrome coronavirus S2 fusion protein., Supekar VM, Bruckmann C, Ingallinella P, Bianchi E, Pessi A, Carfi A, Proc Natl Acad Sci U S A. 2004 Dec 28;101(52):17958-63. Epub 2004 Dec 16. PMID:15604146
Page seeded by OCA on Thu Feb 21 16:37:00 2008
Categories: Protein complex | Bianchi, E. | Bruckmann, C. | Carfi, A. | Ingallinella, P. | Pessi, A. | Supekar, V M. | ACE | NH2 | Coiled coil | Envelope protein | Glycoprotein | Membrane fusion | Sars | Signal | Transmembrane | Viral entry | Virulence
