TY - JOUR
T1 - Mouse lymph node homing receptor cDNA clone encodes a glycoprotein revealing tandem interaction domains
AU - Siegelman, Mark H.
AU - Van De Rijn, Matthijs
AU - Weissman, Irving L.
PY - 1989
Y1 - 1989
N2 - Isolation of a clone encoding the mouse lymph node homing receptor reveals a deduced protein with an unusual protein mosaic architecture, containing a separate carbohydrate-binding (lectin) domain, an epidermal growth factor-like (EGF) domain, and an extracellular precisely duplicated repeat unit, which preserves the motif seen in the homologous repeat structure of complement regulatory proteins and other proteins. The receptor molecule is potentially highly glycosylated, and contains an apparent transmembrane region. Analysis of messenger RNA transcripts reveals a predominantly lymphoid distribution in direct relation to the cell surface expression of the MEL-14 determinant, and the cDNA done is shown to confer the MEL-14 epitope in heterologous cells. The many novel features, induding ubiquitination, embodied in this single receptor molecule form the basis for numerous approaches to the study of cell-cell interactions.
AB - Isolation of a clone encoding the mouse lymph node homing receptor reveals a deduced protein with an unusual protein mosaic architecture, containing a separate carbohydrate-binding (lectin) domain, an epidermal growth factor-like (EGF) domain, and an extracellular precisely duplicated repeat unit, which preserves the motif seen in the homologous repeat structure of complement regulatory proteins and other proteins. The receptor molecule is potentially highly glycosylated, and contains an apparent transmembrane region. Analysis of messenger RNA transcripts reveals a predominantly lymphoid distribution in direct relation to the cell surface expression of the MEL-14 determinant, and the cDNA done is shown to confer the MEL-14 epitope in heterologous cells. The many novel features, induding ubiquitination, embodied in this single receptor molecule form the basis for numerous approaches to the study of cell-cell interactions.
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U2 - 10.1126/science.2646713
DO - 10.1126/science.2646713
M3 - Article
C2 - 2646713
AN - SCOPUS:0024584481
SN - 0036-8075
VL - 243
SP - 1165
EP - 1172
JO - Science
JF - Science
IS - 4895
ER -