6O5E
Crystal structure of the Vitronectin hemopexin-like domain
Summary for 6O5E
| Entry DOI | 10.2210/pdb6o5e/pdb |
| Descriptor | Vitronectin, SODIUM ION, CHLORIDE ION, ... (7 entities in total) |
| Functional Keywords | integrin ligand, hemopexin-like domain, beta-propeller, serum protein, cell adhesion |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 47454.54 |
| Authors | Lechtenberg, B.C.,Shin, K.,Marassi, F.M. (deposition date: 2019-03-01, release date: 2019-09-18, Last modification date: 2024-10-30) |
| Primary citation | Shin, K.,Lechtenberg, B.C.,Fujimoto, L.M.,Yao, Y.,Bartra, S.S.,Plano, G.V.,Marassi, F.M. Structure of human Vitronectin C-terminal domain and interaction withYersinia pestisouter membrane protein Ail. Sci Adv, 5:eaax5068-eaax5068, 2019 Cited by PubMed Abstract: 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 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. PubMed: 31535027DOI: 10.1126/sciadv.aax5068 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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