The Lys (K) residue and residues involved in the aromatic patch are indicated by a closed circle and asterisks, respectively.
Of the 6 aromatic residues that are thought to form an aromatic patch on the surface of these types of protein105, 4 are conserved in the C. tritonis echotoxin-like protein.
Inhibition of AChE and BChE by ethopropazine appears to be sensitive to the nature of the residue corresponding to Phe330 of the aromatic patch in Torpedo spp. AChE and to the volume of the active center in BChE [13], [61].
These residues are spatially close to Y27 and F28 and form a distinct aromatic patch that is solvent exposed (Fig. 1 B).
The observed conformational differences may thus serve to regulate the exposure of the aromatic patch, and the conservation of the patch suggests that it is important, perhaps in interactions with regulatory ligands or with other regions of the full TRPV4 homotetramer.
Superposition of homologous PWWP domains onto the structural model of the complex shows that these domains all share similar configurations of an aromatic cage and basic patches that potentially enable concerted binding to both methylated H3K36 side chain and nucleosomal DNA.
In the process, a patch of aromatic residues is affected, such that a number of these aromatic residues are buried in the presence of ATP.
We show that the LIC G domain binds the dynein heavy chain using a conserved patch of aromatic residues, whereas the less conserved C-terminal domain binds several Rab effectors involved in membrane transport.
This patch contains aromatic residues (black sticks) that would be well placed to interact with conserved prolines in the C-terminal part of the STIL CR2 region that we had to omit for crystallisation.
