Testin - Conformational Change

Conformational Change

Based on the observations that:

  • Mammalian cell derived TES binding Zyxin
  • E. coli produced recombinant TES (rTES) does not bind Zyxin
  • An rTES construct composed of residues 201-421 (i.e., the linker and all 3 LIM domains) does bind Zyxin
  • The above rTES construct binds an N-terminal rTES construct, consisting of the cysteine rich and PET domains - IE, the two halves of TES interact with each other.

Garvalov et al. propose that TES exists in two conformational states: A 'closed' state where the N & C halves of TES interact, obscuring the Zyxin binding site in LIM1, and an 'open' state where the Zyxin binding site is accessible and the two halves no-longer interact in the same fashion, if at all. The regulatory mechanism switching between the two states is not presently fully understood.

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