High-affinity binding to the GM-CSF receptor requires intact N-glycosylation sites in the extracellular domain of the beta subunit.

Abstract

The human granulocyte-macrophage colony-stimulating factor (GM-CSF) receptor consists of 2 glycoprotein subunits, GMRalpha and GMRbeta. GMRalpha in isolation binds to GM-CSF with low affinity. GMRbeta does not bind GM-CSF by itself, but forms a high-affinity receptor in association with GMRalpha. Previously, it was found that N-glycosylation of GMRalpha is… (More)

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Cite this paper

@article{Niu2000HighaffinityBT, title={High-affinity binding to the GM-CSF receptor requires intact N-glycosylation sites in the extracellular domain of the beta subunit.}, author={Lijia Niu and Mark Heaney and Jahaira C Vera and David W. Golde}, journal={Blood}, year={2000}, volume={95 11}, pages={3357-62} }