CRYSTAL STRUCTURE OF THE T1L REOVIRUS ATTACHMENT PROTEIN SIGMA1CRYSTAL STRUCTURE OF THE T1L REOVIRUS ATTACHMENT PROTEIN SIGMA1

Structural highlights

4xc5 is a 3 chain structure with sequence from Mammalian orthoreovirus 1 Lang. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Stettner E, Dietrich MH, Reiss K, Dermody TS, Stehle T. Structure of serotype 1 reovirus attachment protein sigma1 in complex with JAM-A reveals a conserved serotype-independent binding epitope. J Virol. 2015 Mar 25. pii: JVI.00433-15. PMID:25810543 doi:http://dx.doi.org/10.1128/JVI.00433-15

4xc5, resolution 2.20Å

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