Q5F4T5Uniprot
Fold
Class
Family
Origin
Species
Available structures
3ONU : no ligand3ONY : fucose3PA1 : A-type trisaccharide3PA2 : Lewis Y tetrasaccharide3Q38 : B-type trisaccharide3Q39 : H-type disaccharide3Q3A : H-type 2 trisaccharide3Q6Q : no ligand3Q6R : no ligand3RY8 : no ligand4X7E : Nano-854X7F : Nano-254Z4R : Fuc4Z4S : Fuc4Z4T : Fuc4Z4U : Fuc4Z4V : Fuc4Z4W : Fuc4Z4Y : B-type trisaccharide4Z4Z : B-type trisaccharide5BSX : Puregreen245BSY : Lemon juice5HZA : Lewis X trisaccharide5HZB : H-type 2 trisaccharide5O03 : Nano-325O04 : Nano-26 and Nano-855OMM : Nano-145OMN : Nano-276GW1 : glycochenodeoxycholate6GW2 : taurochenodeoxycholate (TCDCA)6GY9 : Fucose derivate8EN2 : Nanobody 34
Related proteins
> 50% identity
> 50% identity
PubMed
Kher G, Sabin C, Lun J, Devant J, Ruoff K, Koromyslova A, von Itzstein M, Pancera M, Hansman G.
Direct Blockade of the Norovirus Histo-Blood Group Antigen Binding Pocket by Nanobodies. Journal of virology 2023
Direct Blockade of the Norovirus Histo-Blood Group Antigen Binding Pocket by Nanobodies. Journal of virology 2023
PubMed
Kilic T, Koromyslova A, Hansman G.
Structural Basis for Human Norovirus Capsid Binding to Bile Acids. Journal of virology 2019
Structural Basis for Human Norovirus Capsid Binding to Bile Acids. Journal of virology 2019
PubMed
Kilic T, Koromyslova A, Hansman G.
Structural Basis for Human Norovirus Capsid Binding to Bile Acids. Journal of virology 2019
Structural Basis for Human Norovirus Capsid Binding to Bile Acids. Journal of virology 2019
PubMed
Bücher K, Yan H, Creutznacher R, Ruoff K, Mallagaray A, Grafmüller A, Dirks J, Kilic T, Weickert S, Rubailo A, Drescher M, Schmidt S, Hansman G, Peters T, Uetrecht C, Hartmann L.
Fucose-Functionalized Precision Glycomacromolecules Targeting Human Norovirus Capsid Protein. Biomacromolecules 2018
Fucose-Functionalized Precision Glycomacromolecules Targeting Human Norovirus Capsid Protein. Biomacromolecules 2018
PubMed
Koromyslova A, Hansman G.
Nanobodies targeting norovirus capsid reveal functional epitopes and potential mechanisms of neutralization. PLoS pathogens 2017
Nanobodies targeting norovirus capsid reveal functional epitopes and potential mechanisms of neutralization. PLoS pathogens 2017
PubMed
Koromyslova A, Hansman G.
Nanobodies targeting norovirus capsid reveal functional epitopes and potential mechanisms of neutralization. PLoS pathogens 2017
Nanobodies targeting norovirus capsid reveal functional epitopes and potential mechanisms of neutralization. PLoS pathogens 2017
PubMed
Koromyslova A, Hansman G.
Nanobodies targeting norovirus capsid reveal functional epitopes and potential mechanisms of neutralization. PLoS pathogens 2017
Nanobodies targeting norovirus capsid reveal functional epitopes and potential mechanisms of neutralization. PLoS pathogens 2017
PubMed
Koromyslova A, Hansman G.
Nanobodies targeting norovirus capsid reveal functional epitopes and potential mechanisms of neutralization. PLoS pathogens 2017
Nanobodies targeting norovirus capsid reveal functional epitopes and potential mechanisms of neutralization. PLoS pathogens 2017
PubMed
Weichert, S., Koromyslova, A., Singh, B.K., Hansman, S., Jennewein, S., Schroten, H., Hansman, G.S.
Structural Basis for Norovirus Inhibition by Human Milk Oligosaccharides. J. Virology 2016
Structural Basis for Norovirus Inhibition by Human Milk Oligosaccharides. J. Virology 2016
PubMed
Weichert, S., Koromyslova, A., Singh, B.K., Hansman, S., Jennewein, S., Schroten, H., Hansman, G.S.
Structural Basis for Norovirus Inhibition by Human Milk Oligosaccharides. J. Virology 2016
Structural Basis for Norovirus Inhibition by Human Milk Oligosaccharides. J. Virology 2016
PubMed
Koromyslova, A.D., Leuthold, M.M., Bowler, M.W., Hansman, G.S.
The sweet quartet: Binding of fucose to the norovirus capsid. Virology 2015
The sweet quartet: Binding of fucose to the norovirus capsid. Virology 2015
PubMed
Koromyslova, A.D., Leuthold, M.M., Bowler, M.W., Hansman, G.S.
The sweet quartet: Binding of fucose to the norovirus capsid. Virology 2015
The sweet quartet: Binding of fucose to the norovirus capsid. Virology 2015
PubMed
Koromyslova, A.D., Leuthold, M.M., Bowler, M.W., Hansman, G.S.
The sweet quartet: Binding of fucose to the norovirus capsid. Virology 2015
The sweet quartet: Binding of fucose to the norovirus capsid. Virology 2015
PubMed
Koromyslova, A.D., Leuthold, M.M., Bowler, M.W., Hansman, G.S.
The sweet quartet: Binding of fucose to the norovirus capsid. Virology 2015
The sweet quartet: Binding of fucose to the norovirus capsid. Virology 2015
PubMed
Koromyslova, A.D., Leuthold, M.M., Bowler, M.W., Hansman, G.S.
The sweet quartet: Binding of fucose to the norovirus capsid. Virology 2015
The sweet quartet: Binding of fucose to the norovirus capsid. Virology 2015
PubMed
Koromyslova, A.D., Leuthold, M.M., Bowler, M.W., Hansman, G.S.
The sweet quartet: Binding of fucose to the norovirus capsid. Virology 2015
The sweet quartet: Binding of fucose to the norovirus capsid. Virology 2015
PubMed
Koromyslova, A.D., Leuthold, M.M., Bowler, M.W., Hansman, G.S.
The sweet quartet: Binding of fucose to the norovirus capsid. Virology 2015
The sweet quartet: Binding of fucose to the norovirus capsid. Virology 2015
PubMed
Koromyslova, A.D., Leuthold, M.M., Bowler, M.W., Hansman, G.S.
The sweet quartet: Binding of fucose to the norovirus capsid. Virology 2015
The sweet quartet: Binding of fucose to the norovirus capsid. Virology 2015
PubMed
Koromyslova A, Hansman G.
Nanobody binding to a conserved epitope promotes norovirus particle disassembly. Journal of virology 2015
Nanobody binding to a conserved epitope promotes norovirus particle disassembly. Journal of virology 2015
PubMed
Koromyslova A, Hansman G.
Nanobody binding to a conserved epitope promotes norovirus particle disassembly. Journal of virology 2015
Nanobody binding to a conserved epitope promotes norovirus particle disassembly. Journal of virology 2015
PubMed
Koromyslova A, White P, Hansman G.
Treatment of norovirus particles with citrate. Virology 2015
Treatment of norovirus particles with citrate. Virology 2015
PubMed
Koromyslova A, White P, Hansman G.
Treatment of norovirus particles with citrate. Virology 2015
Treatment of norovirus particles with citrate. Virology 2015
PubMed
Hansman GS, Shahzad-Ul-Hussan S, McLellan JS, Chuang GY, Georgiev I, Shimoike T, Katayama K, Bewley CA, Kwong PD.
Structural basis for norovirus inhibition and fucose mimicry by citrate. J. Virology 2012
Structural basis for norovirus inhibition and fucose mimicry by citrate. J. Virology 2012
PubMed
Hansman G, Biertümpfel C, Georgiev I, McLellan J, Chen L, Zhou T, Katayama K, Kwong P.
Crystal structures of GII.10 and GII.12 norovirus protruding domains in complex with histo-blood group antigens reveal details for a potential site of vulnerability. Journal of virology 2011
Crystal structures of GII.10 and GII.12 norovirus protruding domains in complex with histo-blood group antigens reveal details for a potential site of vulnerability. Journal of virology 2011
PubMed
Hansman G, Biertümpfel C, Georgiev I, McLellan J, Chen L, Zhou T, Katayama K, Kwong P.
Crystal structures of GII.10 and GII.12 norovirus protruding domains in complex with histo-blood group antigens reveal details for a potential site of vulnerability. Journal of virology 2011
Crystal structures of GII.10 and GII.12 norovirus protruding domains in complex with histo-blood group antigens reveal details for a potential site of vulnerability. Journal of virology 2011
PubMed
Hansman G, Biertümpfel C, Georgiev I, McLellan J, Chen L, Zhou T, Katayama K, Kwong P.
Crystal structures of GII.10 and GII.12 norovirus protruding domains in complex with histo-blood group antigens reveal details for a potential site of vulnerability. Journal of virology 2011
Crystal structures of GII.10 and GII.12 norovirus protruding domains in complex with histo-blood group antigens reveal details for a potential site of vulnerability. Journal of virology 2011
PubMed
Hansman G, Biertümpfel C, Georgiev I, McLellan J, Chen L, Zhou T, Katayama K, Kwong P.
Crystal structures of GII.10 and GII.12 norovirus protruding domains in complex with histo-blood group antigens reveal details for a potential site of vulnerability. Journal of virology 2011
Crystal structures of GII.10 and GII.12 norovirus protruding domains in complex with histo-blood group antigens reveal details for a potential site of vulnerability. Journal of virology 2011
PubMed
Hansman G, Biertümpfel C, Georgiev I, McLellan J, Chen L, Zhou T, Katayama K, Kwong P.
Crystal structures of GII.10 and GII.12 norovirus protruding domains in complex with histo-blood group antigens reveal details for a potential site of vulnerability. Journal of virology 2011
Crystal structures of GII.10 and GII.12 norovirus protruding domains in complex with histo-blood group antigens reveal details for a potential site of vulnerability. Journal of virology 2011
PubMed
Hansman G, Biertümpfel C, Georgiev I, McLellan J, Chen L, Zhou T, Katayama K, Kwong P.
Crystal structures of GII.10 and GII.12 norovirus protruding domains in complex with histo-blood group antigens reveal details for a potential site of vulnerability. Journal of virology 2011
Crystal structures of GII.10 and GII.12 norovirus protruding domains in complex with histo-blood group antigens reveal details for a potential site of vulnerability. Journal of virology 2011
PubMed
Hansman G, Biertümpfel C, Georgiev I, McLellan J, Chen L, Zhou T, Katayama K, Kwong P.
Crystal structures of GII.10 and GII.12 norovirus protruding domains in complex with histo-blood group antigens reveal details for a potential site of vulnerability. Journal of virology 2011
Crystal structures of GII.10 and GII.12 norovirus protruding domains in complex with histo-blood group antigens reveal details for a potential site of vulnerability. Journal of virology 2011
PubMed
Hansman G, Biertümpfel C, Georgiev I, McLellan J, Chen L, Zhou T, Katayama K, Kwong P.
Crystal structures of GII.10 and GII.12 norovirus protruding domains in complex with histo-blood group antigens reveal details for a potential site of vulnerability. Journal of virology 2011
Crystal structures of GII.10 and GII.12 norovirus protruding domains in complex with histo-blood group antigens reveal details for a potential site of vulnerability. Journal of virology 2011
PubMed
Hansman G, Biertümpfel C, Georgiev I, McLellan J, Chen L, Zhou T, Katayama K, Kwong P.
Crystal structures of GII.10 and GII.12 norovirus protruding domains in complex with histo-blood group antigens reveal details for a potential site of vulnerability. Journal of virology 2011
Crystal structures of GII.10 and GII.12 norovirus protruding domains in complex with histo-blood group antigens reveal details for a potential site of vulnerability. Journal of virology 2011
By using this site you agree to our privacy policy.
Please confirm you agree with the privacy policy before using the site.