Final answer:
The bent conformation of an integrin is inactive and cannot bind to its ligand, with its function influenced by mechanical forces and the dynamic equilibrium between affinity states.
Step-by-step explanation:
Evidence strongly suggests that the bent conformation of an integrin is inactive and unable to bind its ligand. Integrins are transmembrane receptors that facilitate cell-extracellular matrix (ECM) adhesion. When integrins are in their bent conformation, they are generally considered to be in a low-affinity state for their ligand, which means they are not in an optimal position to bind.
The models provided by Deshpande and coworkers highlight that there exists a dynamic equilibrium between low and high-affinity states of integrins, with their activation and binding capacity influenced by cellular mechanics such as stress fiber density. When we consider membrane-bound proteins like integrins, it is crucial to understand that their activation state can significantly influence how they interact with ligands, which in turn affects cellular behavior such as adhesion, signaling, and migration.