Structural basis for EGFR ligand sequestration by Argos

Daryl E. Klein, Steven E. Stayrook, Fumin Shi, Kartik Narayan and Mark A. Lemmon ()
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Daryl E. Klein: University of Pennsylvania School of Medicine, 809C Stellar-Chance Laboratories, 422 Curie Boulevard, Philadelphia, Pennsylvania 19104-6059, USA
Steven E. Stayrook: University of Pennsylvania School of Medicine, 809C Stellar-Chance Laboratories, 422 Curie Boulevard, Philadelphia, Pennsylvania 19104-6059, USA
Fumin Shi: University of Pennsylvania School of Medicine, 809C Stellar-Chance Laboratories, 422 Curie Boulevard, Philadelphia, Pennsylvania 19104-6059, USA
Kartik Narayan: University of Pennsylvania School of Medicine, 809C Stellar-Chance Laboratories, 422 Curie Boulevard, Philadelphia, Pennsylvania 19104-6059, USA
Mark A. Lemmon: University of Pennsylvania School of Medicine, 809C Stellar-Chance Laboratories, 422 Curie Boulevard, Philadelphia, Pennsylvania 19104-6059, USA

Nature, 2008, vol. 453, issue 7199, 1271-1275

Abstract: EGFR ligand sequestration by Argos The Drosophila protein Argos is an antagonist of epidermal growth factor receptor (EGFR) signalling that functions by binding and sequestering EGFR ligands. Here the structure of Argos bound to the EGFR ligand Spitz reveals that Argos engulfs the ligand using three related domains with structural resemblance to receptors for TGF-β and urokinase plasminogen activator. These results suggest that undiscovered mammalian counterparts of Argos may exist among other poorly characterized structural homologues. In addition, the structures presented here define requirements for the design of artificial EGF-sequestering proteins that would be valuable anticancer therapeutics.

Date: 2008
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DOI: 10.1038/nature06978

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