Kindlin2
is believed to be crucial in integrin activation, which
mediates the cell–extracellular matrix adhesion and signaling,
but the mechanoregulation of the interaction between Kindlin2 and
integrin remains unclear. Here, we performed the so-called “ramp-clamp”
steered molecular dynamics simulation on the crystal structure of
Kindlin2 bound with β3 integrin. The results showed that the
complex had a better mechanical strength for its rupture force of
about 200 pN under pulling with the velocity of 1 Å/ns, and was
mechanostable for its conformational conservation under constant tensile
force (≤60 pN). The catch-slip bond transition with a force
threshold of 20 pN was demonstrated by the dissociation probability,
the interaction energy, the interface H-bond number, and the force-induced
allostery of the complex. This study might provide a novel insight
into force-dependent Kindlin2/integrin-related signaling and its structural
basis in cellular processes as well as a rational SMD-based computer
strategy for predicting the structure–function relationship
of the stretched complex.