A0A0S4TLR1Uniprot
Fold
Class
Family
Origin
Species
Available structures
Related proteins
> 50% identity
> 50% identity
PubMed
Ramberg K, Guagnini F, Engilberge S, Wronska M, Rennie M, Pérez J, Crowley P.
Segregated Protein-Cucurbit(7)uril Crystalline Architectures via Modulatory Peptide Tectons. Chemistry (Weinheim an der Bergstrasse, Germany) 2021
Segregated Protein-Cucurbit(7)uril Crystalline Architectures via Modulatory Peptide Tectons. Chemistry (Weinheim an der Bergstrasse, Germany) 2021
PubMed
Houser J, Kozmon S, Mishra D, Hammerová Z, Wimmerová M, Koca J.
The CH-pi Interaction in Protein-Carbohydrate Binding: Bioinformatics and In Vitro Quantification. Chemistry (Weinheim an der Bergstrasse, Germany) 2020
The CH-pi Interaction in Protein-Carbohydrate Binding: Bioinformatics and In Vitro Quantification. Chemistry (Weinheim an der Bergstrasse, Germany) 2020
PubMed
Houser J, Kozmon S, Mishra D, Hammerová Z, Wimmerová M, Koca J.
The CH-pi Interaction in Protein-Carbohydrate Binding: Bioinformatics and In Vitro Quantification. Chemistry (Weinheim an der Bergstrasse, Germany) 2020
The CH-pi Interaction in Protein-Carbohydrate Binding: Bioinformatics and In Vitro Quantification. Chemistry (Weinheim an der Bergstrasse, Germany) 2020
PubMed
Houser J, Kozmon S, Mishra D, Hammerová Z, Wimmerová M, Koca J.
The CH-pi Interaction in Protein-Carbohydrate Binding: Bioinformatics and In Vitro Quantification. Chemistry (Weinheim an der Bergstrasse, Germany) 2020
The CH-pi Interaction in Protein-Carbohydrate Binding: Bioinformatics and In Vitro Quantification. Chemistry (Weinheim an der Bergstrasse, Germany) 2020
PubMed
Tobola F, Lelimousin M, Varrot A, Gillon E, Darnhofer B, Blixt O, Birner-Gruenberger R, Imberty A, Wiltschi B.
Effect of Noncanonical Amino Acids on Protein-Carbohydrate Interactions: Structure, Dynamics, and Carbohydrate Affinity of a Lectin Engineered with Fluorinated Tryptophan Analogs. ACS chemical biology 2018
Effect of Noncanonical Amino Acids on Protein-Carbohydrate Interactions: Structure, Dynamics, and Carbohydrate Affinity of a Lectin Engineered with Fluorinated Tryptophan Analogs. ACS chemical biology 2018
PubMed
Tobola F, Lelimousin M, Varrot A, Gillon E, Darnhofer B, Blixt O, Birner-Gruenberger R, Imberty A, Wiltschi B.
Effect of Noncanonical Amino Acids on Protein-Carbohydrate Interactions: Structure, Dynamics, and Carbohydrate Affinity of a Lectin Engineered with Fluorinated Tryptophan Analogs. ACS chemical biology 2018
Effect of Noncanonical Amino Acids on Protein-Carbohydrate Interactions: Structure, Dynamics, and Carbohydrate Affinity of a Lectin Engineered with Fluorinated Tryptophan Analogs. ACS chemical biology 2018
PubMed
Tobola F, Lelimousin M, Varrot A, Gillon E, Darnhofer B, Blixt O, Birner-Gruenberger R, Imberty A, Wiltschi B.
Effect of Noncanonical Amino Acids on Protein-Carbohydrate Interactions: Structure, Dynamics, and Carbohydrate Affinity of a Lectin Engineered with Fluorinated Tryptophan Analogs. ACS chemical biology 2018
Effect of Noncanonical Amino Acids on Protein-Carbohydrate Interactions: Structure, Dynamics, and Carbohydrate Affinity of a Lectin Engineered with Fluorinated Tryptophan Analogs. ACS chemical biology 2018
PubMed
Topin, J., Lelimousin, M., Arnaud, J., Audfray, A., Perez, S., Varrot, A., Imberty, A.
Literature The Hidden Conformation of Lewis X, a Human Histo-Blood Group Antigen, is a Determinant for Recognition by Pathogen Lectins Acs Chem.Biol. 2016
Literature The Hidden Conformation of Lewis X, a Human Histo-Blood Group Antigen, is a Determinant for Recognition by Pathogen Lectins Acs Chem.Biol. 2016
PubMed
Topin, J., Lelimousin, M., Arnaud, J., Audfray, A., Perez, S., Varrot, A., Imberty, A.
Literature The Hidden Conformation of Lewis X, a Human Histo-Blood Group Antigen, is a Determinant for Recognition by Pathogen Lectins Acs Chem.Biol. 2016
Literature The Hidden Conformation of Lewis X, a Human Histo-Blood Group Antigen, is a Determinant for Recognition by Pathogen Lectins Acs Chem.Biol. 2016
PubMed
Kostlanova N, Mitchell EP, Lortat-Jacob H, Oscarson S, Lahmann M, Gilboa-Garber N, Chambat G, Wimmerova M, Imberty A.
The fucose-binding lectin from Ralstonia solanacearum. A new type of beta-propeller architecture formed by oligomerization and interacting with fucoside, fucosyllactose, and plant xyloglucan J. Biol. Chem. 2005
The fucose-binding lectin from Ralstonia solanacearum. A new type of beta-propeller architecture formed by oligomerization and interacting with fucoside, fucosyllactose, and plant xyloglucan J. Biol. Chem. 2005
PubMed
Kostlanova N, Mitchell EP, Lortat-Jacob H, Oscarson S, Lahmann M, Gilboa-Garber N, Chambat G, Wimmerova M, Imberty A.
The fucose-binding lectin from Ralstonia solanacearum. A new type of beta-propeller architecture formed by oligomerization and interacting with fucoside, fucosyllactose, and plant xyloglucan J. Biol. Chem. 2005
The fucose-binding lectin from Ralstonia solanacearum. A new type of beta-propeller architecture formed by oligomerization and interacting with fucoside, fucosyllactose, and plant xyloglucan J. Biol. Chem. 2005
PubMed
Kostlanova N, Mitchell EP, Lortat-Jacob H, Oscarson S, Lahmann M, Gilboa-Garber N, Chambat G, Wimmerova M, Imberty A.
The fucose-binding lectin from Ralstonia solanacearum. A new type of beta-propeller architecture formed by oligomerization and interacting with fucoside, fucosyllactose, and plant xyloglucan J. Biol. Chem. 2005
The fucose-binding lectin from Ralstonia solanacearum. A new type of beta-propeller architecture formed by oligomerization and interacting with fucoside, fucosyllactose, and plant xyloglucan J. Biol. Chem. 2005
PubMed
Kostlanova N, Mitchell EP, Lortat-Jacob H, Oscarson S, Lahmann M, Gilboa-Garber N, Chambat G, Wimmerova M, Imberty A.
The fucose-binding lectin from Ralstonia solanacearum. A new type of beta-propeller architecture formed by oligomerization and interacting with fucoside, fucosyllactose, and plant xyloglucan J. Biol. Chem. 2005
The fucose-binding lectin from Ralstonia solanacearum. A new type of beta-propeller architecture formed by oligomerization and interacting with fucoside, fucosyllactose, and plant xyloglucan J. Biol. Chem. 2005
By using this site you agree to our privacy policy.
Please confirm you agree with the privacy policy before using the site.