Immunoglobulin-binding domains: Protein L from Peptostreptococcus magnus.

@article{Housden2003ImmunoglobulinbindingDP,
  title={Immunoglobulin-binding domains: Protein L from Peptostreptococcus magnus.},
  author={N. G. Housden and S. Harrison and S. E. Roberts and J. A. Beckingham and M. Graille and E. Stura and M. Gore},
  journal={Biochemical Society transactions},
  year={2003},
  volume={31 Pt 3},
  pages={
          716-8
        }
}
Protein L is a multidomain cell-wall protein isolated from Peptostreptococcus magnus. It belongs to a group of proteins that contain repeated domains that are able to bind to Igs without stimulating an immune response, the most characterized of this group being Protein A ( Staphylococcus aureus ) and Protein G ( Streptococcus ). Both of these proteins bind predominantly to the interface of C(H)2-C(H)3 heavy chains, while Protein L binds exclusively to the V(L) domain of the kappa -chain. The… Expand
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References

SHOWING 1-6 OF 6 REFERENCES
Bacterial immunoglobulin-binding proteins—future trends
TLDR
The driving force for any practical application involving bacterial immunoglobulin-binding proteins will be directed toward identifying the problem, determining the limitations of current reagents, and modifying or finding new reagents that will achieve the desired result. Expand
Biochemistry
The Department of Biochemistry is internationally recognized for its research and education and offers a world-class interdisciplinary research environment in a beautiful mountain setting. As part of… Expand
  • 1995
J. Mol. Biol. Eur. J. Biochem. Structure J. Biol. Chem. Biochem. J
  • J. Mol. Biol. Eur. J. Biochem. Structure J. Biol. Chem. Biochem. J
  • 1995
Biochemistry J. Biol. Chem. Mol. Microbiol
  • Biochemistry J. Biol. Chem. Mol. Microbiol
  • 1992
J. Mol. Biol
  • J. Mol. Biol
  • 1992