Structures of adnectin/protein complexes reveal an expanded binding footprint.

@article{Ramamurthy2012StructuresOA,
  title={Structures of adnectin/protein complexes reveal an expanded binding footprint.},
  author={Vidhyashankar Ramamurthy and Stanley R. Krystek and Alexander M Bush and Anzhi Wei and Stuart L Emanuel and Ruchira Das Gupta and Ahsen Janjua and Lin Cheng and Melissa Murdock and Bozena M Abramczyk and Daniel J. Cohen and Zheng Jiong Lin and Paul J. Morin and Jonathan Davis and Michael Dabritz and Douglas C McLaughlin and Katie A Russo and Ginger Chao and Martin C Wright and Victoria A Jenny and Linda J. Engle and Eric S Furfine and Steven Sheriff},
  journal={Structure},
  year={2012},
  volume={20 2},
  pages={259-69}
}
Adnectins are targeted biologics derived from the tenth type III domain of human fibronectin (¹⁰Fn3), a member of the immunoglobulin superfamily. Target-specific binders are selected from libraries generated by diversifying the three ¹⁰Fn3 loops that are analogous to the complementarity determining regions of antibodies. The crystal structures of two Adnectins were determined, each in complex with its therapeutic target, EGFR or IL-23. Both Adnectins bind different epitopes than those bound by… CONTINUE READING