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1kke

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Revision as of 06:54, 11 August 2021

Crystal Structure of Reovirus Attachment Protein Sigma1 Trimer

Structural highlights

1kke is a 3 chain structure with sequence from Mammalian orthoreovirus 3 strain dearing. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SIGM1_REOVD] 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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Reovirus attaches to cellular receptors with the sigma1 protein, a fiber-like molecule protruding from the 12 vertices of the icosahedral virion. The crystal structure of a receptor-binding fragment of sigma1 reveals an elongated trimer with two domains: a compact head with a new beta-barrel fold and a fibrous tail containing a triple beta-spiral. Numerous structural and functional similarities between reovirus sigma1 and the adenovirus fiber suggest an evolutionary link in the receptor-binding strategies of these two viruses. A prominent loop in the sigma1 head contains a cluster of residues that are conserved among reovirus serotypes and are likely to form a binding site for junction adhesion molecule, an integral tight junction protein that serves as a reovirus receptor. The fibrous tail is mainly responsible for sigma1 trimer formation, and it contains a highly flexible region that allows for significant movement between the base of the tail and the head. The architecture of the trimer interface and the observed flexibility indicate that sigma1 is a metastable structure poised to undergo conformational changes upon viral attachment and cell entry.

Crystal structure of reovirus attachment protein sigma1 reveals evolutionary relationship to adenovirus fiber.,Chappell JD, Prota AE, Dermody TS, Stehle T EMBO J. 2002 Jan 15;21(1-2):1-11. PMID:11782420^[1]

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

References

↑ Chappell JD, Prota AE, Dermody TS, Stehle T. Crystal structure of reovirus attachment protein sigma1 reveals evolutionary relationship to adenovirus fiber. EMBO J. 2002 Jan 15;21(1-2):1-11. PMID:11782420 doi:http://dx.doi.org/10.1093/emboj/21.1.1

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1kke"

@@ Line 3: / Line 3: @@
 <StructureSection load='1kke' size='340' side='right'caption='[[1kke]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1kke]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Mammalian_orthoreovirus_3_strain_dearing Mammalian orthoreovirus 3 strain dearing]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KKE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1kke]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mammalian_orthoreovirus_3_strain_dearing Mammalian orthoreovirus 3 strain dearing]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KKE FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kke OCA], [http://pdbe.org/1kke PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kke RCSB], [http://www.ebi.ac.uk/pdbsum/1kke PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kke ProSAT]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kke OCA], [https://pdbe.org/1kke PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kke RCSB], [https://www.ebi.ac.uk/pdbsum/1kke PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kke ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SIGM1_REOVD SIGM1_REOVD]] 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.
+[[https://www.uniprot.org/uniprot/SIGM1_REOVD SIGM1_REOVD]] 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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 30: @@
 ==See Also==
 *[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
+*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
 == References ==
 <references/>

1kke

From Proteopedia

Revision as of 06:54, 11 August 2021

Crystal Structure of Reovirus Attachment Protein Sigma1 Trimer

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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