4xc5

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== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/SIGM1_REOVL SIGM1_REOVL]] Fiber-like molecule that attaches the virion to the host cell membrane by binding to the primary receptor F11R/JAM-A and to sialic acid containing proteins (coreceptor). The interaction of sigma-1 with F11R is required for NF-kB activation and apoptosis. Binding to both sialic acid and F11R is required to induce maximal levels of apoptosis (By similarity).
[[http://www.uniprot.org/uniprot/SIGM1_REOVL SIGM1_REOVL]] Fiber-like molecule that attaches the virion to the host cell membrane by binding to the primary receptor F11R/JAM-A and to sialic acid containing proteins (coreceptor). The interaction of sigma-1 with F11R is required for NF-kB activation and apoptosis. Binding to both sialic acid and F11R is required to induce maximal levels of apoptosis (By similarity).
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== Publication Abstract from PubMed ==
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Mammalian orthoreoviruses use glycans and junctional adhesion molecule-A (JAM-A) as attachment receptors. We determined the structure of serotype 1 reovirus attachment protein sigma1 alone and in complex with JAM-A. Comparison with the structure of serotype 3 reovirus sigma1 bound to JAM-A reveals that both sigma1 proteins engage JAM-A with similar affinities and via conserved binding epitopes. Thus, sigma1-JAM-A interactions are unlikely to explain the differences in pathogenesis displayed by these reovirus serotypes.
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Structure of serotype 1 reovirus attachment protein sigma1 in complex with JAM-A reveals a conserved serotype-independent binding epitope.,Stettner E, Dietrich MH, Reiss K, Dermody TS, Stehle T J Virol. 2015 Mar 25. pii: JVI.00433-15. PMID:25810543<ref>PMID:25810543</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
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<references/>
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Revision as of 05:33, 8 April 2015

CRYSTAL STRUCTURE OF THE T1L REOVIRUS ATTACHMENT PROTEIN SIGMA1

4xc5, resolution 2.20Å

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