Vitronectin (Vn) is a major component of blood that controls many processes central to
human biology. It is a drug target and a key factor in cell and tissue engineering
applications, but despite long-standing efforts, little is known about the molecular basis for its
functions. Here, we define the domain organization of Vn, report the crystal structure of its
carboxyl-terminal domain, and show that it harbors the binding site for the Yersinia pestis
outer membrane protein Ail, which recruits Vn to the bacterial cell surface to evade human …

Vitronectin (Vn) is a major component of blood that controls many processes central to
human biology. It is a drug target and a key factor in cell and tissue engineering
applications, but despite long-standing efforts, little is known about the molecular basis for its
functions. Here, we define the domain organization of Vn, report the crystal structure of its
carboxyl-terminal domain, and show that it harbors the binding site for the Yersinia pestis
outer membrane protein Ail, which recruits Vn to the bacterial cell surface to evade human …