Structure of the collagen-binding domain from a Staphylococcus aureus adhesin

@article{Symersky1997StructureOT,
  title={Structure of the collagen-binding domain from a Staphylococcus aureus adhesin},
  author={Jindrich Symersky and Joseph M. Patti and Mike Carson and Karen House-Pompeo and Michael Teale and Dwight D Moore and Lei Jin and Amy Schneider and Lawrence J Delucas and Magnus H{\"o}{\"o}k and Sthanam V. L. Narayana},
  journal={Nature Structural Biology},
  year={1997},
  volume={4},
  pages={833-838}
}
The crystal structure of the recombinant 19,000 Mr binding domain from the Staphylococcus aureus collagen adhesin has been determined at 2 Å resolution. The domain fold is a jelly-roll, composed of two antiparallel β-sheets and two short α-helices. Triple-helical collagen model probes were used in a systematic docking search to identify the collagen-binding site. A groove on β-sheet I exhibited the best surface complementarity to the collagen probes. This site partially overlaps with the… CONTINUE READING

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