Background: Helicobacter pylori SabA outer membrane protein is crucial for the bacteria to adhere to host stomach surface during chronic infection. Results: The structure of the extracellular SabA adhesion region is determined by x-ray crystallography. Conclusion: SabA adhesion structure may provide insight into binding sites important for ligand receptor interactions. Significance: SabA is the first reported extracellular domain structure of the H. pylori outer membrane protein family. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.
CITATION STYLE
Pang, S. S., Nguyen, S. T. S., Perry, A. J., Day, C. J., Panjikar, S., Tiralongo, J., … Kwok, T. (2014). The three-dimensional structure of the extracellular adhesion domain of the sialic acid-binding adhesin SabA from Helicobacter pylori. Journal of Biological Chemistry, 289(10), 6332–6340. https://doi.org/10.1074/jbc.M113.513135
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