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Fruit fly protein acts as decoy to capture tumor growth factors, find Penn researchers
Date:5/28/2008

gues have worked out the details of the three-dimensional structure of Argos when it binds to Spitz. "We were surprised to find that Argos has three very similar domains that capture Spitz by surrounding it like a C-clamp," explains Lemmon. Although Argos binding to Spitz mimics the characteristic binding of EGFR to EGF, Argos and EGFR do not share the same amino acid sequence or structural similarities.

The structure of Argos was studied by X-ray crystallography, a technique that shows where each atom of the protein is located. Computer analysis is then used to put together all the data into a three-dimensional projection of the growth factor and its binding molecule.

The next step is to identify a human protein that is similar in structure to Argos. Intriguingly, Argos shares structural similarities with the human receptors for transforming growth factor and urokinase plasminogen activator. "There are quite a few other human proteins with similar predicted structures whose function is not yet known," says Lemmon. "We think that one of these might be a functional analogue of Argos, and we could exploit that as a drug."


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Contact: Karen Kreeger
karen.kreeger@uphs.upenn.edu
215-349-5658
University of Pennsylvania School of Medicine
Source:Eurekalert  

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