Team develops first 3D look at interaction between immune sensor and protein that helps bacteria move.
To invade organisms such as humans, bacteria make use of a protein called flagellin, part of a tail-like appendage that helps the bacteria move about. Now, for the first time, a team led by scientists at The Scripps Research Institute and Sanford-Burnham Medical Research Institute has determined the 3D structure of the interaction between this critical bacterial protein and an immune molecule called TLR5, shedding light on how the body protects itself from such foreign invaders.
The study, published February 17 in Science, not only helps decipher the molecular mechanism underlying TLR5 recognition and function, but it also advances knowledge that’s key to the design of new therapeutics.
Click "source" for entire article.
Science - "Structural Basis of TLR5-Flagellin Recognition and Signaling" (http://www.sciencemag.org/content/335/6070/859)
To invade organisms such as humans, bacteria make use of a protein called flagellin, part of a tail-like appendage that helps the bacteria move about. Now, for the first time, a team led by scientists at The Scripps Research Institute and Sanford-Burnham Medical Research Institute has determined the 3D structure of the interaction between this critical bacterial protein and an immune molecule called TLR5, shedding light on how the body protects itself from such foreign invaders.
The study, published February 17 in Science, not only helps decipher the molecular mechanism underlying TLR5 recognition and function, but it also advances knowledge that’s key to the design of new therapeutics.
Click "source" for entire article.
Science - "Structural Basis of TLR5-Flagellin Recognition and Signaling" (http://www.sciencemag.org/content/335/6070/859)
