The rationale is that, if homologs of both partners are present in different species, it is likely that they interact in a similar manner and that the residues contributing to this interaction will be under evolutionary constraints that can be detected in the sequence alignment.
Both extracellular and transmembrane (TM) glycoprotein domains contribute to this interaction, but study of TM TM interactions has been limited because synthesis and structural characterization of these highly hydrophobic segments present significant challenges.
Moreover, a region within the C-terminal GTPase domain of Gαo appears to contribute to this interaction.
The high negative charge of the DNA in the SL-DNA conjugate contributes to this interaction, enhancing binding affinity.
However, as already anticipated in the Introduction, several lines of evidence indicate that Bub1 contributes to this interaction (Discussion).
Notably, however, the crystal structure suggests additional residues in the N-terminus of Bub1 contribute to this interaction.
Structural studies also uncovered that the F2 lobe of the Krit1 FERM domain also contributes to this interaction.
Although carrier sires of the BMP15 mutation are systematically discarded from breeding, this mutation is still present in the female population and might contribute to this interaction.
Taken together, these results support the notion that TSAd and Nck interact in vivo, and that both Nck SH2 and SH3 domains contribute to this interaction.
In the nACh, 5-HT3, MOD-1, glycine glycine, and GluCl receptors one of these amino acids has been shown to form a cation−π interaction with agonist, while two aromatics contribute to this interaction in an insect GABA receptor.
