A cysteine-rich domain of the “mannose” receptor mediates GalNAc-4-SO4 binding
DJ Fiete, MC Beranek… - Proceedings of the …, 1998 - National Acad Sciences
DJ Fiete, MC Beranek, JU Baenziger
Proceedings of the National Academy of Sciences, 1998•National Acad SciencesA critical element of lutropin bioactivity in vivo is its rapid removal from the blood by a
receptor, located in hepatic endothelial cells, that recognizes the terminal sulfated
carbohydrate structure SO4-4-GalNAcβ1, 4GlcNAcβ1, 2Manα (S4GGnM). We have
previously shown that the macrophage mannose (Man)-receptor cDNA directs the synthesis
of a protein that binds oligosaccharides with either terminal S4GGnM or terminal Man, at
independent sites. We now show that the cysteine-rich (Cys-Rich) domain at the N terminus …
receptor, located in hepatic endothelial cells, that recognizes the terminal sulfated
carbohydrate structure SO4-4-GalNAcβ1, 4GlcNAcβ1, 2Manα (S4GGnM). We have
previously shown that the macrophage mannose (Man)-receptor cDNA directs the synthesis
of a protein that binds oligosaccharides with either terminal S4GGnM or terminal Man, at
independent sites. We now show that the cysteine-rich (Cys-Rich) domain at the N terminus …
A critical element of lutropin bioactivity in vivo is its rapid removal from the blood by a receptor, located in hepatic endothelial cells, that recognizes the terminal sulfated carbohydrate structure SO4-4-GalNAcβ1,4GlcNAcβ1,2Manα (S4GGnM). We have previously shown that the macrophage mannose (Man)-receptor cDNA directs the synthesis of a protein that binds oligosaccharides with either terminal S4GGnM or terminal Man, at independent sites. We now show that the cysteine-rich (Cys-Rich) domain at the N terminus of the Man/S4GGnM receptor accounts for binding of oligosaccharides with terminal GalNAc-4-SO4, whereas calcium-dependent carbohydrate recognition domains (CRDs) account for binding of ligands containing terminal Man. The Cys-Rich domain is thus a previously unrecognized carbohydrate binding motif. Cys-Rich domains have been described on the three other members of the endocytic C-type lectin family of receptors. The structural relationship of these receptors to the Man/S4GGnM receptor raises the possibility that their Cys-Rich domains also bind carbohydrate moieties and contribute to their function.
National Acad Sciences