Filtern
Volltext vorhanden
- nein (1)
Erscheinungsjahr
- 2008 (1)
Dokumenttyp
Sprache
- Englisch (1)
Gehört zur Bibliographie
- ja (1)
Institut
- Institut für Biochemie und Biologie (1) (entfernen)
The tailspike protein P22 recognizes an octasaccharide derived from the O-antigen polysaccharide of Salmonella enteritidis in a shallow groove and molecular docking successfully identifies this binding region on the protein surface. Analysis by 2D 1H,1H-T-ROESY and transferred NOESY NMR experiments indicate that the bound octasaccharide ligand has a conformation similar to that observed in solution. The results from a saturation transfer difference NMR experiment show that a large number of protons in the octasaccharide are in close contact with the protein as a result of binding. A comparison of the crystal structure of the complex and a molecular dynamics simulation of the octasaccharide with explicit water molecules suggest that only minor conformational changes are needed upon binding to the tailspike protein.