2b4h

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[[Image:2b4h.gif|left|200px]]
[[Image:2b4h.gif|left|200px]]
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{{Structure
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|PDB= 2b4h |SIZE=350|CAPTION= <scene name='initialview01'>2b4h</scene>, resolution 1.6&Aring;
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The line below this paragraph, containing "STRUCTURE_2b4h", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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|GENE= GENOME SEGMENT 4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10969 Rhesus rotavirus])
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|DOMAIN=
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{{STRUCTURE_2b4h| PDB=2b4h | SCENE= }}
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|RELATEDENTRY=[[1slq|1SLQ]], [[2b4h|2B4H]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b4h OCA], [http://www.ebi.ac.uk/pdbsum/2b4h PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2b4h RCSB]</span>
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'''Crystal Structure of the Rhesus Rotavirus VP5 Antigen Domain Dimer'''
'''Crystal Structure of the Rhesus Rotavirus VP5 Antigen Domain Dimer'''
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[[Category: Dormitzer, P R.]]
[[Category: Dormitzer, P R.]]
[[Category: Yoder, J D.]]
[[Category: Yoder, J D.]]
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[[Category: beta sandwich]]
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[[Category: Beta sandwich]]
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[[Category: greek key]]
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[[Category: Greek key]]
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[[Category: membrane penetration protein]]
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[[Category: Membrane penetration protein]]
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[[Category: non-enveloped virus]]
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[[Category: Non-enveloped virus]]
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[[Category: rearrangement]]
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[[Category: Rearrangement]]
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[[Category: spike protein]]
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[[Category: Spike protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:50:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:01:26 2008''
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Revision as of 16:50, 3 May 2008

Image:2b4h.gif

Template:STRUCTURE 2b4h

Crystal Structure of the Rhesus Rotavirus VP5 Antigen Domain Dimer


Overview

The spike protein VP4 is a key component of the membrane penetration apparatus of rotavirus, a nonenveloped virus that causes childhood gastroenteritis. Trypsin cleavage of VP4 produces a fragment, VP5*, with a potential membrane interaction region, and primes rotavirus for cell entry. During entry, the part of VP5* that protrudes from the virus folds back on itself and reorganizes from a local dimer to a trimer. Here, we report that a globular domain of VP5*, the VP5* antigen domain, is an autonomously folding unit that alternatively forms well-ordered dimers and trimers. Because the domain contains heterotypic neutralizing epitopes and is soluble when expressed directly, it is a promising potential subunit vaccine component. X-ray crystal structures show that the dimer resembles the spike body on trypsin-primed virions, and the trimer resembles the folded-back form of the spike. The same structural elements pack differently to form key intermolecular contacts in both oligomers. The intrinsic molecular property of alternatively forming dimers and trimers facilitates the VP5* reorganization, which is thought to mediate membrane penetration during cell entry.

About this Structure

2B4H is a Single protein structure of sequence from Rhesus rotavirus. Full crystallographic information is available from OCA.

Reference

Alternative intermolecular contacts underlie the rotavirus VP5* two- to three-fold rearrangement., Yoder JD, Dormitzer PR, EMBO J. 2006 Apr 5;25(7):1559-68. Epub 2006 Mar 2. PMID:16511559 Page seeded by OCA on Sat May 3 19:50:40 2008

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