Contribution to ligand binding by multiple carbohydrate-recognition domains in the macrophage mannose receptor.
ME Taylor, K Bezouska, K Drickamer - Journal of Biological Chemistry, 1992 - ASBMB
The extracellular portion of the macrophage mannose receptor is composed of several
cysteine-rich domains, including a fibronectin type II repeat and eight segments related in
sequence to Ca (2+)-dependent carbohydrate-recognition domains (CRDs) of animal
lectins. Expression of portions of the receptor in vitro, in fibroblasts and in bacteria, has been
used to determine which of the extracellular domains are involved in binding and
endocytosis of ligand. The NH2-terminal cysteine-rich domain and the fibronectin type II …
cysteine-rich domains, including a fibronectin type II repeat and eight segments related in
sequence to Ca (2+)-dependent carbohydrate-recognition domains (CRDs) of animal
lectins. Expression of portions of the receptor in vitro, in fibroblasts and in bacteria, has been
used to determine which of the extracellular domains are involved in binding and
endocytosis of ligand. The NH2-terminal cysteine-rich domain and the fibronectin type II …