1slq: Difference between revisions

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[[Image:1slq.gif|left|200px]]
{{Seed}}
[[Image:1slq.png|left|200px]]


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{{STRUCTURE_1slq|  PDB=1slq  |  SCENE=  }}  
{{STRUCTURE_1slq|  PDB=1slq  |  SCENE=  }}  


'''Crystal structure of the trimeric state of the rhesus rotavirus VP4 membrane interaction domain, VP5CT'''
===Crystal structure of the trimeric state of the rhesus rotavirus VP4 membrane interaction domain, VP5CT===




==Overview==
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Non-enveloped virus particles (those that lack a lipid-bilayer membrane) must breach the membrane of a target host cell to gain access to its cytoplasm. So far, the molecular mechanism of this membrane penetration step has resisted structural analysis. The spike protein VP4 is a principal component in the entry apparatus of rotavirus, a non-enveloped virus that causes gastroenteritis and kills 440,000 children each year. Trypsin cleavage of VP4 primes the virus for entry by triggering a rearrangement that rigidifies the VP4 spikes. We have determined the crystal structure, at 3.2 A resolution, of the main part of VP4 that projects from the virion. The crystal structure reveals a coiled-coil stabilized trimer. Comparison of this structure with the two-fold clustered VP4 spikes in a approximately 12 A resolution image reconstruction from electron cryomicroscopy of trypsin-primed virions shows that VP4 also undergoes a second rearrangement, in which the oligomer reorganizes and each subunit folds back on itself, translocating a potential membrane-interaction peptide from one end of the spike to the other. This rearrangement resembles the conformational transitions of membrane fusion proteins of enveloped viruses.
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{{ABSTRACT_PUBMED_15329727}}


==About this Structure==
==About this Structure==
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[[Category: Non-enveloped virus]]
[[Category: Non-enveloped virus]]
[[Category: Spike protein]]
[[Category: Spike protein]]
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