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

Preprint

15 August 2007

preprint
Published by arXiv in arXiv

https://doi.org/10.48550/arXiv.0708.2083

Abstract

E. Coli. dihydrofolate reductase (DHFR) undergoes conformational transitions between the closed (CS) and occluded (OS) states which, respectively, describe whether the active site is closed or occluded by the Met20 loop. A sequence-based approach is used to identify a network of residues that represents the allostery wiring diagram. We also use a self-organized polymer model to monitor the kinetics of the CS->OS and the reverse transitions. a sliding motion of Met20 loop is observed. The residues that facilitate the Met20 loop motion are part of the network of residues that transmit allosteric signals during the CS->OS transition.

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