1zv8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1zv8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zv8, resolution 1.94&Aring;" /> '''A structure-based me...)
Line 1: Line 1:
-
[[Image:1zv8.gif|left|200px]]<br /><applet load="1zv8" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1zv8.gif|left|200px]]<br /><applet load="1zv8" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1zv8, resolution 1.94&Aring;" />
caption="1zv8, resolution 1.94&Aring;" />
'''A structure-based mechanism of SARS virus membrane fusion'''<br />
'''A structure-based mechanism of SARS virus membrane fusion'''<br />
==Overview==
==Overview==
-
Entry of SARS coronavirus into its target cell requires large-scale, structural transitions in the viral spike (S) glycoprotein in order to, induce fusion of the virus and cell membranes. Here we describe the, identification and crystal structures of four distinct alpha-helical, domains derived from the highly conserved heptad-repeat (HR) regions of, the S2 fusion subunit. The four domains are an antiparallel four-stranded, coiled coil, a parallel trimeric coiled coil, a four-helix bundle, and a, six-helix bundle that is likely the final fusogenic form of the protein., When considered together, the structural and thermodynamic features of the, four domains suggest a possible mechanism whereby the HR regions, initially sequestered in the native S glycoprotein spike, are released and, refold sequentially to promote membrane fusion. Our results provide a, structural framework for understanding the control of membrane fusion and, should guide efforts to intervene in the SARS coronavirus entry process.
+
Entry of SARS coronavirus into its target cell requires large-scale structural transitions in the viral spike (S) glycoprotein in order to induce fusion of the virus and cell membranes. Here we describe the identification and crystal structures of four distinct alpha-helical domains derived from the highly conserved heptad-repeat (HR) regions of the S2 fusion subunit. The four domains are an antiparallel four-stranded coiled coil, a parallel trimeric coiled coil, a four-helix bundle, and a six-helix bundle that is likely the final fusogenic form of the protein. When considered together, the structural and thermodynamic features of the four domains suggest a possible mechanism whereby the HR regions, initially sequestered in the native S glycoprotein spike, are released and refold sequentially to promote membrane fusion. Our results provide a structural framework for understanding the control of membrane fusion and should guide efforts to intervene in the SARS coronavirus entry process.
==About this Structure==
==About this Structure==
-
1ZV8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_sars_coronavirus Human sars coronavirus] and [http://en.wikipedia.org/wiki/Sars_coronavirus Sars coronavirus] with CAC, ACT, ZN and NA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZV8 OCA].
+
1ZV8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_sars_coronavirus Human sars coronavirus] and [http://en.wikipedia.org/wiki/Sars_coronavirus Sars coronavirus] with <scene name='pdbligand=CAC:'>CAC</scene>, <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZV8 OCA].
==Reference==
==Reference==
Line 31: Line 31:
[[Category: virus entry]]
[[Category: virus entry]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:40:57 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:19:23 2008''

Revision as of 14:19, 21 February 2008

Image:1zv8.gif

1zv8, resolution 1.94Å

Drag the structure with the mouse to rotate

A structure-based mechanism of SARS virus membrane fusion

Overview

Entry of SARS coronavirus into its target cell requires large-scale structural transitions in the viral spike (S) glycoprotein in order to induce fusion of the virus and cell membranes. Here we describe the identification and crystal structures of four distinct alpha-helical domains derived from the highly conserved heptad-repeat (HR) regions of the S2 fusion subunit. The four domains are an antiparallel four-stranded coiled coil, a parallel trimeric coiled coil, a four-helix bundle, and a six-helix bundle that is likely the final fusogenic form of the protein. When considered together, the structural and thermodynamic features of the four domains suggest a possible mechanism whereby the HR regions, initially sequestered in the native S glycoprotein spike, are released and refold sequentially to promote membrane fusion. Our results provide a structural framework for understanding the control of membrane fusion and should guide efforts to intervene in the SARS coronavirus entry process.

About this Structure

1ZV8 is a Protein complex structure of sequences from Human sars coronavirus and Sars coronavirus with , , and as ligands. Full crystallographic information is available from OCA.

Reference

Structures and polymorphic interactions of two heptad-repeat regions of the SARS virus S2 protein., Deng Y, Liu J, Zheng Q, Yong W, Lu M, Structure. 2006 May;14(5):889-99. PMID:16698550

Page seeded by OCA on Thu Feb 21 16:19:23 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1zv8"
Personal tools