6o5e
Crystal structure of the Vitronectin hemopexin-like domainCrystal structure of the Vitronectin hemopexin-like domain
Structural highlights
FunctionVTNC_HUMAN Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway. Somatomedin-B is a growth hormone-dependent serum factor with protease-inhibiting activity. Publication Abstract from PubMedVitronectin (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 beta/alpha-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. Structure of human Vitronectin C-terminal domain and interaction with Yersinia pestis outer membrane protein Ail.,Shin K, Lechtenberg BC, Fujimoto LM, Yao Y, Bartra SS, Plano GV, Marassi FM Sci Adv. 2019 Sep 11;5(9):eaax5068. doi: 10.1126/sciadv.aax5068. eCollection 2019, Sep. PMID:31535027[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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