scholarly journals X-ray Crystal Structure of the Human Galectin-3 Carbohydrate Recognition Domain at 2.1-Å Resolution

1998 ◽  
Vol 273 (21) ◽  
pp. 13047-13052 ◽  
Author(s):  
J. Seetharaman ◽  
Amit Kanigsberg ◽  
Rita Slaaby ◽  
Hakon Leffler ◽  
Samuel H. Barondes ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Carbohydrate Recognition Domain ◽  
Carbohydrate Recognition ◽  
X Ray ◽  
Galectin 3

Crystal Structure of the Carbohydrate Recognition Domain of the H1 Subunit of the Asialoglycoprotein Receptor

2000 ◽  
Vol 300 (4) ◽  
pp. 857-865 ◽  
Author(s):  
Markus Meier ◽  
Marc D. Bider ◽  
Vladimir N. Malashkevich ◽  
Martin Spiess ◽  
Peter Burkhard
Keyword(s):  
Crystal Structure ◽  
Asialoglycoprotein Receptor ◽  
Carbohydrate Recognition Domain ◽  
Carbohydrate Recognition

scholarly journals Peptides derived from human galectin-3 N-terminal tail interact with its carbohydrate recognition domain in a phosphorylation-dependent manner

2014 ◽  
Vol 443 (1) ◽  
pp. 126-131 ◽  
Author(s):  
M. Álvaro Berbís ◽  
Sabine André ◽  
F. Javier Cañada ◽  
Rüdiger Pipkorn ◽  
Hans Ippel ◽  
...  
Keyword(s):  
Carbohydrate Recognition Domain ◽  
Dependent Manner ◽  
Carbohydrate Recognition ◽  
Galectin 3

scholarly journals Protein Flexibility and Conformational Entropy in Ligand Design Targeting the Carbohydrate Recognition Domain of Galectin-3

2010 ◽  
Vol 132 (41) ◽  
pp. 14577-14589 ◽  
Author(s):  
Carl Diehl ◽  
Olof Engström ◽  
Tamara Delaine ◽  
Maria Håkansson ◽  
Samuel Genheden ◽  
...  
Keyword(s):  
Protein Flexibility ◽  
Ligand Design ◽  
Carbohydrate Recognition Domain ◽  
Carbohydrate Recognition ◽  
Conformational Entropy ◽  
Galectin 3

scholarly journals A bivalent glycopeptide to target two putative carbohydrate binding sites on FimH

2010 ◽  
Vol 6 ◽  
pp. 801-809 ◽  
Author(s):  
Thisbe K Lindhorst ◽  
Kathrin Bruegge ◽  
Andreas Fuchs ◽  
Oliver Sperling
Keyword(s):  
Binding Site ◽  
Binding Sites ◽  
Carbohydrate Binding ◽  
Carbohydrate Recognition Domain ◽  
Carbohydrate Recognition ◽  
Binding Studies ◽  
Bivalent Ligand ◽  
X Ray ◽  
Carbohydrate Binding Site

FimH is a mannose-specific bacterial lectin found on type 1 fimbriae with a monovalent carbohydrate recognition domain (CRD) that is known from X-ray studies. However, binding studies with multivalent ligands have suggested an additional carbohydrate-binding site on this protein. In order to prove this hypothesis, a bivalent glycopeptide ligand with the capacity to bridge two putative carbohydrate binding sites on FimH was designed and synthesized. Anti-adhesion assays with the new bivalent ligand and type 1-fimbriated bacteria have revealed, that verification of the number of carbohydrate binding sites on FimH with a tailor-made bivalent glycopeptide requires further investigation to be conclusive.

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