TY  - JOUR
A1  - Landström, Jens
A1  - Nordmark, Eva-Lisa
A1  - Eklund, Robert
A1  - Weintraub, Andrej
A1  - Seckler, Robert
A1  - Widmalm, Göran
T1  - Interaction of a Salmonella enteritidis O-antigen octasaccharide with the phage P22 tailspike protein by NMR spectroscopy and docking studies
N2  - 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.
Y1  - 2008
UR  - http://www.springerlink.com/content/w3146138p25r2456/
U6  - https://doi.org/10.1007/s10719-007-9065-9
SN  - 0282-0080
ER  -