Sandbox Reserved 1771: Difference between revisions

Many transmembrane interactions can be found within a IgM BCR. The <scene name='95/952699/Transmembrane_region/3'>α and β subunits</scene> have numerous interactions that keep them associated with each other. Residue interactions found within the α-β subunits, such as hydrogen bonds, ionic interactions, and hydrophobic interactions between nonpolar residues can be found <scene name='95/952699/Overview_hbonds_fixed/6'>here</scene>. At cellular pH, charged residues found in the transmembrane region strengthen the overall interaction through hydrogen bonds and ionic interactions.  For example, <scene name='95/952699/N155_e138_hbonds_fixed/6'>a hydrogen bond</scene> between residues N155 and E138, along with numerous other hydrogen bonds, works to stabilize the α-β chain interactions in the transmembrane region. Further down the chains, <scene name='95/952699/T166_e148_hbonds_fixed/6'>hydrogen bonding</scene> between residues T166 and E148 work to keep the α-β subunit associated with each other. Overall, these hydrogen bonds and ion interactions work to maintain the association of the α-β chains, which allows the BCR to activate an immune response.