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InterPro: IPR009013 Viral attachment protein, fibre shaft

Protein matchesHelp
UniProtKB
Matches:
354 proteins
AccessionHelp IPR009013 Viral_attachment_fibre_shaft
TypeHelp Repeat
SignaturesHelp
InterPro RelationshipsHelp
Children IPR000939 Adenoviral fiber protein, repeat/shaft region
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 attachment proteins in adenoviruses and reoviruses display structural similarity, indicating similar cell-surface receptor binding strategies, even though these viruses differ from one another in design, capsid composition and genome composition [1, 2]. The dsDNA adenoviruses are responsible for diseases such as pneumonia, cystitis, conjunctivitis and diarrhoea, all of which can be fatal to patients who are immunocompromised, while the dsRNA reoviruses are responsible for mild respiratory or gastrointestinal infections.

The attachment proteins play a pivotal role in disease patterns through their selective recognition of cell-surface receptors. The fibre protein and the sigma 1 protein act as attachment proteins in adenoviruses and reoviruses, respectively. The attachment proteins are homo-trimeric, and contain a long, thin central shaft, or tail domain, and a C-terminal head domain that plays an important role in cell attachment. The structure of the shaft or tail domain reveals a triple beta-spiral that is formed by interlocking beta-hairpin repeat units.

Structural linksHelp

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR009013 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. van Raaij MJ, Mitraki A, Lavigne G, Cusack S.
A triple beta-spiral in the adenovirus fibre shaft reveals a new structural motif for a fibrous protein.
Nature 401 935-8 1999 [PubMed: 10553913]
http://dx.doi.org/10.1038/44880
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

Additional ReadingHelp
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
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 2001 302-12 [PubMed: 11437664]
http://dx.doi.org/10.1006/viro.2001.0967
Papanikolopoulou K, Teixeira S, Belrhali H, Forsyth VT, Mitraki A, van Raaij MJ.
Adenovirus fibre shaft sequences fold into the native triple beta-spiral fold when N-terminally fused to the bacteriophage T4 fibritin foldon trimerisation motif.
J. Mol. Biol. 342 2004 219-27 [PubMed: 15313619]
http://dx.doi.org/10.1016/j.jmb.2004.07.008
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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InterPro 23.1