1jmu: Difference between revisions

Revision as of 21:25, 2 May 2008

Crystal Structure of the Reovirus mu1/sigma3 Complex

OverviewOverview

Cell entry by nonenveloped animal viruses requires membrane penetration without membrane fusion. The reovirus penetration agent is the outer-capsid protein, Mu1. The structure of Mu1, complexed with its "protector" protein, Sigma3, and the fit of this Mu1(3)Sigma3(3) heterohexameric complex into the cryoEM image of an intact virion, reveal molecular events essential for viral penetration. Autolytic cleavage divides Mu1 into myristoylated Mu1N and Mu1C. A long hydrophobic pocket can receive the myristoyl group. Dissociation of Mu1N, linked to a major conformational change of the entire Mu1 trimer, must precede myristoyl-group insertion into the cellular membrane. A myristoyl switch, coupling exposure of the fatty acid chain, autolytic cleavage of Mu1N, and long-range molecular rearrangement of Mu1C, thus appears to be part of the penetration mechanism.

About this StructureAbout this Structure

1JMU is a Protein complex structure of sequences from Reovirus sp.. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the reovirus membrane-penetration protein, Mu1, in a complex with is protector protein, Sigma3., Liemann S, Chandran K, Baker TS, Nibert ML, Harrison SC, Cell. 2002 Jan 25;108(2):283-95. PMID:11832217 Page seeded by OCA on Fri May 2 21:25:38 2008

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OCA

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 '''Crystal Structure of the Reovirus mu1/sigma3 Complex'''
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 [[Category: Liemann, S.]]
 [[Category: Nibert, M L.]]
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