Low force (left) favors dissociation of selectin (pink) from its ligand (blue). More force opens the selectin hinge and allows the ligand to slide into new interactions (right).

Leukocytes are more likely to grab onto a vascular surface when under flow than in the absence of flow. This counterintuitive behavior relies on bonds between transmembrane selectins on the blood cell and their vascular ligands. These so-called “catch bonds” get stronger because flow flips open selectin into a binding-ready conformation, Lou et al. show on page 1107.

The authors have solved the structure of L-selectin, which can now be added to previous structures of P- and E-selectin. The extracellular domains of all three have an N-terminal lectin domain and an EGF-like domain that are separated by a hinge. In L- and E-selectin, the two sides of this hinge are connected by a hydrogen bond between...

You do not currently have access to this content.