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.
Read more about this topic: Testin
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