To prevent unregulated adhesion, most integrins are expressed in an inactive form. EM and crystal structures showed that the extracellular domain of the integrin αVβ3 without its ligand can assume a bent conformation. 2D EM reconstructions of the same domain in the presence of a small peptide suggested that the bound form, in contrast, was extended. These results supported a switchblade model, in which the binding of cytoplasmic signals initiates the movement of several intra- and extracellular domains that opens and activates the integrin by exposing its ligand-binding site.
But Adair et al. suggest that such large-scale...
The Rockefeller University Press
2005
The Rockefeller University Press
2005
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