Solution NMR Evidence for Symmetry in Functionally or Crys-tallographically Asymmetric Homodimers
David Travis Gallagher, Raquel Godoy-Ruiz, Anna Krejcirikova, Vitali Tugarinov
A recurrent theme of many structural studies of homo-oligomeric protein systems is concerned with verification that the conformation observed in a crystal repre¬sents the functionally relevant structure. An asymmetric con-formation adopted by two chemically identical subunits in homo-oligomers can represent an intrinsic property of a protein or be an artifact induced by crystal packing forces. Solution NMR studies can distinguish between these two possibilities. Using methyl-based NMR spectroscopy we provide evidence for symmetry in the absence of ligands in several homodimeric proteins that are either asymmetric functionally and/or adopt different conformations of the two subunits in available x-ray structures.
, Godoy-Ruiz, R.
, Krejcirikova, A.
and Tugarinov, V.
Solution NMR Evidence for Symmetry in Functionally or Crys-tallographically Asymmetric Homodimers, Journal of the American Chemical Society, [online], https://doi.org/10.1021/ja206967d
(Accessed March 4, 2024)