In these cells, rHu BChE was expressed as mostly tetrameric form by the simultaneous expression of proline-rich attachment domain.
These structures lacked the C-terminal amphipathic t-peptide (WAT domain) that interacts with the proline-rich attachment domain (PRAD).
The C-terminal ∼40-residue t-peptide (9, 10), also called the tryptophan amphiphilic tetramerization (WAT) domain, interacts with the proline-rich attachment domain (PRAD) of the collagen-like Q subunit (ColQ).
Chains E−H (numbered I−IV, respectively) of the tetrameric AChE C-terminal region and chain J (numbered V) of the proline-rich attachment domain (PRAD) of the ColQ protein were extracted from the crystal structure (PDB entry 1VZJ).
This association is facilitated by interaction between the tryptophan amphiphilic tetramerization domains on the catalytic subunits of AChE and the proline-rich attachment domain (PRAD) on the extracellular domain of PRIMA1.
However, there is an X-ray crystal structure [Protein Data Bank (PDB) entry 1VZJ] of the isolated tetrameric C-terminal association domain of AChE in complex with a proline-rich attachment domain (PRAD) of the protein ColQ (10).
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AChET is capable of forming G1a, G2a, and G4na [29], as well as "tailed" forms (thus the T subunit) by associating with a transmembrane protein, the Proline-Rich Membrane Attachment (PRiMA) [30] and the triple helical collagen Q (ColQ; Q for queue, tail in French) [31], [32].
This notion is supported by the observation that Arabidopsis thaliana AHL1 binds to the AT-rich scaffold/matrix attachment regions (S/MARs) and its AT-hook motif is indispensable for AHL1's DNA binding capacity [ 32].
This may indicate a scale-free scenario, reflecting an environment of 'rich get richer' through preferential attachment (Barabási and Bonabeau 2003).
