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Flexible neck in cell-receptor DC-SIGN targets more pathogens
Date:7/14/2009

and posted on the journal's Web site.

From their force-distance measurements the researchers determined DC-SIGN's neck length as 28 nanometers (a nanometer is 1 billionth of a meter), in agreement with hydrodynamic measurements and theoretical estimates by other researchers, which placed the neck length between 20 and 30 nanometers.

When the protein binds to a pathogen, binding sites on the cell receptor rearrange slightly, to adapt to the target surface and maximize the bond. This 5 nanometer conformational change is binding-induced, and made possible by a flexible linker in the neck, the researchers report.

"The protein neck region acts as a stiff, but flexible, rod that projects the molecule's binding sites away from the cell surface," Leckband said. "A rigid presentation of the binding sites at the end of the neck would restrict DC-SIGN to a few specific, spatial forms. Instead, the molecule's flexibility and adaptability allow it to recognize a much wider range of pathogens."


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Contact: James E. Kloeppel
kloeppel@illinois.edu
217-244-1073
University of Illinois at Urbana-Champaign
Source:Eurekalert

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