Sandbox Reserved 1771: Difference between revisions

Line 17:

===Transmembrane Interactions===

Many transmembrane interactions can be found within a IgM BCR. The <scene name='95/952699/Transmembrane_region/2'>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 and ionic interactions can be found <scene name='95/952699/Overview_hbonds_fixed/3'>here</scene> (highlighted in green). At cellular pH, charged residues found in the transmembrane region strengthen the overall interaction through hydrogen bonds and ionic interactions. Additionally, hydrophobic interactions between isoleucine residues are present which further contribute to the overall interaction between the subunits. For example, <scene name='95/952699/N155_e138_hbonds_fixed/3'>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/4'>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.

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 and ionic interactions can be found <scene name='95/952699/Overview_hbonds_fixed/4'>here</scene> (highlighted in green). At cellular pH, charged residues found in the transmembrane region strengthen the overall interaction through hydrogen bonds and ionic interactions. Additionally, hydrophobic interactions between isoleucine residues are present which further contribute to the overall interaction between the subunits. For example, <scene name='95/952699/N155_e138_hbonds_fixed/4'>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/5'>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.

==Structure Summary==

Sandbox Reserved 1771: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 17: / Line 17: @@
 ===Transmembrane Interactions===
-Many transmembrane interactions can be found within a IgM BCR. The <scene name='95/952699/Transmembrane_region/2'>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 and ionic interactions can be found <scene name='95/952699/Overview_hbonds_fixed/3'>here</scene> (highlighted in green). At cellular pH, charged residues found in the transmembrane region strengthen the overall interaction through hydrogen bonds and ionic interactions. Additionally, hydrophobic interactions between isoleucine residues are present which further contribute to the overall interaction between the subunits. For example, <scene name='95/952699/N155_e138_hbonds_fixed/3'>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/4'>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.
+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 and ionic interactions can be found <scene name='95/952699/Overview_hbonds_fixed/4'>here</scene> (highlighted in green). At cellular pH, charged residues found in the transmembrane region strengthen the overall interaction through hydrogen bonds and ionic interactions. Additionally, hydrophobic interactions between isoleucine residues are present which further contribute to the overall interaction between the subunits. For example, <scene name='95/952699/N155_e138_hbonds_fixed/4'>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/5'>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.
 ==Structure Summary==