2hsq

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[[Image:2hsq.gif|left|200px]]
[[Image:2hsq.gif|left|200px]]
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{{Structure
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|PDB= 2hsq |SIZE=350|CAPTION= <scene name='initialview01'>2hsq</scene>, resolution 3.97&Aring;
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The line below this paragraph, containing "STRUCTURE_2hsq", creates the "Structure Box" on the page.
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|GENE= VCL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), ipaA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=623 Shigella flexneri])
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{{STRUCTURE_2hsq| PDB=2hsq | SCENE= }}
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|RELATEDENTRY=[[2gww|2GWW]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hsq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hsq OCA], [http://www.ebi.ac.uk/pdbsum/2hsq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hsq RCSB]</span>
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'''Human vinculin (head domain, Vh1, residues 1-258) in complex with Shigella's IpaA vinculin binding site 2 (residues 565-587)'''
'''Human vinculin (head domain, Vh1, residues 1-258) in complex with Shigella's IpaA vinculin binding site 2 (residues 565-587)'''
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[[Category: Shigella flexneri]]
[[Category: Shigella flexneri]]
[[Category: Izard, T.]]
[[Category: Izard, T.]]
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[[Category: protein complex]]
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[[Category: Protein complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:39:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:34:53 2008''
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Revision as of 03:39, 4 May 2008

Template:STRUCTURE 2hsq

Human vinculin (head domain, Vh1, residues 1-258) in complex with Shigella's IpaA vinculin binding site 2 (residues 565-587)


Contents

Overview

Shigella flexneri, the causative agent of bacillary dysentery, injects invasin proteins through a type III secretion apparatus upon contacting the host cell, which triggers pathogen internalization. The invasin IpaA is essential for S. flexneri pathogenesis and binds to the cytoskeletal protein vinculin to facilitate host cell entry. We report that IpaA harbors two vinculin-binding sites (VBSs) within its C-terminal domain that bind to and activate vinculin in a mutually exclusive fashion. Only the highest affinity C-terminal IpaA VBS is necessary for efficient entry and cell-cell spread of S. flexneri, whereas the lower affinity VBS appears to contribute to vinculin recruitment at entry foci of the pathogen. Finally, the crystal structures of vinculin in complex with the VBSs of IpaA reveal the mechanism by which IpaA subverts vinculin's functions, where S. flexneri utilizes a remarkable level of molecular mimicry of the talin-vinculin interaction to activate vinculin. Mimicry of vinculin's interactions may therefore be a general mechanism applied by pathogens to infect the host cell.

Disease

Known disease associated with this structure: Cardiomyopathy, dilated, 1W OMIM:[193065]

About this Structure

2HSQ is a Protein complex structure of sequences from Homo sapiens and Shigella flexneri. Full crystallographic information is available from OCA.

Reference

Shigella applies molecular mimicry to subvert vinculin and invade host cells., Izard T, Tran Van Nhieu G, Bois PR, J Cell Biol. 2006 Nov 6;175(3):465-75. PMID:17088427 Page seeded by OCA on Sun May 4 06:39:56 2008

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