A Specific Antibody to the Carbohydrate Recognition Domain of the Asialoglycoprotein Receptor RHL1 Subunit Does Not React with RHL2/3 but Blocks Ligand Binding

1998 ◽  
Vol 249 (1) ◽  
pp. 236-240
Author(s):  
Fu-Yue Zeng ◽  
Janet A. Oka ◽  
Paul H. Weigel
Keyword(s):  
Ligand Binding ◽  
Specific Antibody ◽  
Asialoglycoprotein Receptor ◽  
Carbohydrate Recognition Domain ◽  
Carbohydrate Recognition

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

Characterization of residues and sequences of the carbohydrate recognition domain required for cell surface localization and ligand binding of human lectin-like oxidized LDL receptor

2001 ◽  
Vol 114 (7) ◽  
pp. 1273-1282
Author(s):  
X. Shi ◽  
S. Niimi ◽  
T. Ohtani ◽  
S. Machida
Keyword(s):  
Cell Surface ◽  
Ligand Binding ◽  
Disulfide Bonds ◽  
Oxidized Ldl ◽  
Ldl Receptor ◽  
Density Lipoprotein ◽  
Carbohydrate Recognition Domain ◽  
Carbohydrate Recognition ◽  
Surface Localization ◽  
Cell Surface Localization

Lectin-like oxidized low-density lipoprotein receptor (LOX-1) has been cloned from human aortic endothelial cells, and has a sequence identical to that from human lung. Previous studies showed that human LOX-1 can recognize modified LDL, apoptotic cells and bacteria. To further explore the relationship between the structure and function of LOX-1, a mutagenesis study was carried out. Our results showed that the carbohydrate recognition domain (CRD) was the ligand-binding domain of human LOX-1. We also investigated the sequences and residues in CRD that were essential for protein cell surface localization and ligand binding. LOX-1s carrying a mutation on each of six Cys in CRD resulted in a variety of N-glycosylation and failed to be transported to the cell surface. This was strong evidence for the involvement of all six Cys in the intrachain disulfide bonds required for proper folding, processing and transport of LOX-1. The C-terminal sequence (KANLRAQ) was also essential for protein folding and transport, while the four final residues (LRAQ) were involved in maintaining receptor function. Both positive charged (R208, R209, H226, R229 and R231) and non-charged hydrophilic (Q193, S198, S199 and N210) residues were involved in ligand binding, suggesting that ligand recognition of LOX-1 is not merely dependent on the interaction of positively charged residues with negatively charged ligands.

The Carbohydrate-Recognition Domain of E-Selectin Is Sufficient for Ligand Binding under Both Static and Flow Conditions

Biochemistry ◽  
1996 ◽  
Vol 35 (20) ◽  
pp. 6385-6392 ◽  
Author(s):  
Frank Kolbinger ◽  
John T. Patton ◽  
Gabi Geisenhoff ◽  
Anja Aenis ◽  
Xiaohong Li ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Carbohydrate Recognition Domain ◽  
Flow Conditions ◽  
Carbohydrate Recognition

scholarly journals Ligand Binding and Signaling of Dendritic Cell Immunoreceptor (DCIR) Is Modulated by the Glycosylation of the Carbohydrate Recognition Domain

PLoS ONE ◽  
2013 ◽  
Vol 8 (6) ◽  
pp. e66266 ◽  
Author(s):  
Karien Bloem ◽  
Ilona M. Vuist ◽  
Arend-Jan van der Plas ◽  
Léon M. J. Knippels ◽  
Johan Garssen ◽  
...  
Keyword(s):  
Dendritic Cell ◽  
Ligand Binding ◽  
Carbohydrate Recognition Domain ◽  
Carbohydrate Recognition
Sign in / Sign up

Export Citation Format

Share Document