Structural Comparison of ATP-binding Effects

From WakeDEAC

An illustration of the structural effects of ATP binding on DNA-bound MutS structures. The binding of a second ATP to MutS causes conformational changes, illustrated by color, blue for the largest conformational changes, green for intermediate changes and red for the smallest changes. The MutS comples is the prokaryotic equivalent to the MSH2/MSH6 complex, which are key mismatch repair proteins functioning in both cell death and repair pathways. Conformational changes in MSH proteins are critical to the regulation of these pathways.

This research was conducted on the DEAC cluster by Professor Salsbury of the Physics department who collaborates with the Scarpinato Lab in the Cancer Biology department.