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InterPro: IPR008982 Viral attachment protein

Protein matchesHelp
UniProtKB
Matches:
304 proteins
AccessionHelp IPR008982 Viral_att
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Children IPR000978 Adenoviral fiber protein, knob
Found in IPR000931 Adenovirus fibre protein
IPR002592 Viral attachment sigma 1, reoviral
GO Term annotationHelp
Process GO:0007155 cell adhesion
GO:0008037 cell recognition
GO:0019058 viral infectious cycle
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

The viral attachment protein domain forms part of the fibre proteins in adenoviruses [1], and the sigma 1 protein in reoviruses [2]. Both proteins are trimers that contain fibrous tails and globular heads (reovirus), or knobs (adenovirus), which are structurally very similar. Both domain cores consist of eight anti-parallel beta-sheets, forming either a beta sandwich (fibre knob), or a beta-barrel (sigma 1 head), with a long loop containing an alpha helix. The remaining loops tend to be longer in the fibre knob. Functionally both the fibre knob and the sigma 1 head are involved in binding selectively to cell surface receptors. The reoviruses bind JAM (junction adhesion molecule), while the adenoviruses use the CAR (Coxsackievirus and adenovirus) receptor, with the exception of subgroup B adenoviruses [3].

Structural linksHelp

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR008982 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P03275 Fiber protein

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR008982 Viral attachment protein
IPR000978 Adenoviral fiber protein, knob
IPR000931 Adenovirus fibre protein
IPR009013 Viral attachment protein, fibre shaft
IPR000939 Adenoviral fiber protein, repeat/shaft region
PDB Chain
ModBase
CATH Domain
SCOP Domain

PublicationsHelp
1. Bewley MC, Springer K, Zhang YB, Freimuth P, Flanagan JM.
Structural analysis of the mechanism of adenovirus binding to its human cellular receptor, CAR.
Science 286 1579-83 1999 [PubMed: 10567268]
http://dx.doi.org/10.1126/science.286.5444.1579
2. Chappell JD, Prota AE, Dermody TS, Stehle T.
Crystal structure of reovirus attachment protein sigma1 reveals evolutionary relationship to adenovirus fiber.
EMBO J. 21 1-11 2002 [PubMed: 11782420]
http://dx.doi.org/10.1093/emboj/21.1.1
3. Durmort C, Stehlin C, Schoehn G, Mitraki A, Drouet E, Cusack S, Burmeister WP.
Structure of the fiber head of Ad3, a non-CAR-binding serotype of adenovirus.
Virology 285 302-12 2001 [PubMed: 11437664]
http://dx.doi.org/10.1006/viro.2001.0967

Additional ReadingHelp
Persson BD, Reiter DM, Marttila M, Mei YF, Casasnovas JM, Arnberg N, Stehle T.
Adenovirus type 11 binding alters the conformation of its receptor CD46.
Nat. Struct. Mol. Biol. 14 2007 164-6 [PubMed: 17220899]
http://dx.doi.org/10.1038/nsmb1190
Papanikolopoulou K, Forge V, Goeltz P, Mitraki A.
Formation of highly stable chimeric trimers by fusion of an adenovirus fiber shaft fragment with the foldon domain of bacteriophage t4 fibritin.
J. Biol. Chem. 279 2004 8991-8 [PubMed: 14699113]
http://dx.doi.org/10.1074/jbc.M311791200
Seiradake E, Lortat-Jacob H, Billet O, Kremer EJ, Cusack S.
Structural and mutational analysis of human Ad37 and canine adenovirus 2 fiber heads in complex with the D1 domain of coxsackie and adenovirus receptor.
J. Biol. Chem. 281 2006 33704-16 [PubMed: 16923808]
http://dx.doi.org/10.1074/jbc.M605316200
Wang H, Liaw YC, Stone D, Kalyuzhniy O, Amiraslanov I, Tuve S, Verlinde CL, Shayakhmetov D, Stehle T, Roffler S, Lieber A.
Identification of CD46 binding sites within the adenovirus serotype 35 fiber knob.
J. Virol. 81 2007 12785-92 [PubMed: 17898059]
http://dx.doi.org/10.1128/JVI.01732-07
Burmeister WP, Guilligay D, Cusack S, Wadell G, Arnberg N.
Crystal structure of species D adenovirus fiber knobs and their sialic acid binding sites.
J. Virol. 78 2004 7727-36 [PubMed: 15220447]
http://dx.doi.org/10.1128/JVI.78.14.7727-7736.2004
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