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E. Coli. dihydrofolate reductase (DHFR) undergoes conformational transitionsbetween the closed (CS) and occluded (OS) states which, respectively, describewhether the active site is closed or occluded by the Met20 loop. Asequence-based approach is used to identify a network of residues thatrepresents the allostery wiring diagram. We also use a self-organized polymermodel to monitor the kinetics of the CS->OS and the reverse transitions. asliding motion of Met20 loop is observed. The residues that facilitate theMet20 loop motion are part of the network of residues that transmit allostericsignals during the CS->OS transition.

Allosteric communication in Dihydrofolate Reductase: Signaling network and pathways for closed to occluded transition and back