Anticalins: exploiting a non-Ig scaffold with hypervariable loops for the engineering of binding proteins.

@article{Richter2014AnticalinsEA,
  title={Anticalins: exploiting a non-Ig scaffold with hypervariable loops for the engineering of binding proteins.},
  author={Antonia Richter and Evelyn Eggenstein and Arne Skerra},
  journal={FEBS letters},
  year={2014},
  volume={588 2},
  pages={
          213-8
        }
}
Antibodies, which can recognize a plethora of possible antigens, have been considered as a paradigm of protein engineering performed by nature itself. Lipocalins constitute a distinct family of proteins with functions in ligand binding and transport that occur in many organisms, including man. Like antibodies, lipocalins exhibit a structurally conserved framework - a β-barrel with an attached α-helix - which supports four structurally hypervariable loops forming a cup-shaped binding site. Thus… CONTINUE READING

Citations

Publications citing this paper.
SHOWING 1-10 OF 34 CITATIONS

Anticalin® Proteins as Therapeutic Agents in Human Diseases

VIEW 2 EXCERPTS
CITES BACKGROUND & METHODS

References

Publications referenced by this paper.
SHOWING 1-10 OF 41 REFERENCES

CTLA-4 blockade and the renaissance of cancer immunotherapy.

VIEW 1 EXCERPT