Structure of human Vitronectin C-terminal domain and interaction with Yersinia pestis outer membrane protein Ail. Sci Adv 2019 Sep;5(9):eaax5068
Date
09/20/2019Pubmed ID
31535027Pubmed Central ID
PMC6739113DOI
10.1126/sciadv.aax5068Scopus ID
2-s2.0-85072215989 (requires institutional sign-in at Scopus site) 15 CitationsAbstract
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 host defenses. Vn forms a single four-bladed β/α-propeller that serves as a hub for multiple functions. The structure explains key features of native Vn and provides a blueprint for understanding and targeting this essential human protein.
Author List
Shin K, Lechtenberg BC, Fujimoto LM, Yao Y, Bartra SS, Plano GV, Marassi FMAuthors
Francesca M. Marassi PhD Chair, Professor in the Biophysics department at Medical College of WisconsinKyungsoo Shin PhD Assistant Professor in the Biophysics department at Medical College of Wisconsin
MESH terms used to index this publication - Major topics in bold
Amino Acid SequenceBacterial Outer Membrane Proteins
Binding Sites
Crystallography, X-Ray
Humans
Protein Binding
Protein Conformation
Sequence Homology
Virulence Factors
Vitronectin
Yersinia pestis
