|
||
Journal of Experimental Medicine, Vol 166, 1055-1069, Copyright © 1987 by Rockefeller University Press
ARTICLES |
HM Wang and KA Smith
Department of Medicine, Dartmouth Medical School, Hanover, New Hampshire 03756.
High-affinity IL-2-R binding results from an exceptional type of cooperative interaction between two IL-2-binding proteins termed alpha and beta. When expressed together on the cell surface, these two distinct chains form a noncovalent kinetic hybrid receptor complex that exploits a rapid association rate contributed by the p55 beta chain and a slow dissociation rate characteristic for the p75 alpha chain. The p75 alpha chains signal cell growth, whereas the p55 beta chains only facilitate IL-2 binding by serving as helper binding sites, having no discernible signaling role themselves. The unique functional implications of this structural organization indicate that this cooperative bimolecular arrangement reflects a general mechanism by which the efficiency of surface receptors can be enhanced markedly.
This article has been cited by other articles:
| TABLE OF CONTENTS |
|