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InterPro: IPR000939 Adenoviral fiber protein, repeat/shaft region

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UniProtKB

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322 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession

IPR000939 Adenobir_fiber_prot_rpt/shaft

Type

Repeat

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00608	Adeno_shaft	322
Signatures in BioMart

InterPro Relationships Help

Parent

IPR009013 Viral attachment protein, fibre shaft

Found in

IPR000931 Adenovirus fibre protein

GO Term annotation Help

Process

GO:0007155 cell adhesion
GO:0008037 cell recognition
GO:0009405 pathogenesis

InterPro annotation

Entry Details in BioMart

Abstract

Adenoviruses are responsible for diseases such as pneumonia, cystitis, conjunctivitis and diarrhoea, all of which can be fatal to patients who are immunocompromised [1]. Viral infection commences with recognition of host cell receptors by means of specialised proteins on viral surfaces. Specific attachment of adenovirus is achieved through interactions between host-cell receptors and the adenovirus fiber protein and is mediated by the globular carboxy-terminal domain of the adenovirus fiber protein, rather than the 'shaft' region represented by this family. The alignment of this family contains two copies of a fifteen residue repeat found in the 'shaft' region of adenoviral fiber proteins.

Structural links Help

PDB - click here

SCOP: b.83.1.1

Database links Help

PANDIT: PF00608

Blocks: IPB000939

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR000939

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

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

Publications Open in usermanual
1.	Xia D, Henry LJ, Gerard RD, Deisenhofer J. Crystal structure of the receptor-binding domain of adenovirus type 5 fiber protein at 1.7 A resolution. Structure 2 1259-70 1994 [PubMed: 7704534] http://dx.doi.org/10.1016/S0969-2126(94)00126-X

Additional Reading Open in usermanual
	Kidd AH, Erasmus MJ. Sequence characterization of the adenovirus 40 fiber gene. Virology 172 1989 134-44 [PubMed: 2773314] http://dx.doi.org/10.1016/0042-6822(89)90115-3
	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
	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 1999 935-8 [PubMed: 10553913] http://dx.doi.org/10.1038/44880
	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
	Strelkov SV, Tao Y, Shneider MM, Mesyanzhinov VV, Rossmann MG. Structure of bacteriophage T4 fibritin M: a troublesome packing arrangement. Acta Crystallogr. D Biol. Crystallogr. 54 1998 805-16 [PubMed: 9757094] http://dx.doi.org/10.1107/S0907444997018878

InterPro 23.1