Sandbox Reserved 1785: Difference between revisions

Line 16:

===Transmembrane Region===

The IgM BCR is tethered to [https://en.wikipedia.org/wiki/B_cell B-cell] membranes through the <scene name='95/952714/Integral_region/2'>transmembrane region </scene> which is broken up into both extracellular and integral domains. IgM BCR assembly requires dimerization of the Ig alpha and Ig beta subunits which embed within the B-cell membrane. The <scene name='95/952714/Ig_alpha_beta/1'> Ig alpha and beta heterodimer </scene> is dimerized in both the integral region, with a hydrogen bond, and within the extracellular region with a <scene name='95/952714/Extracellular_disulfide_bridge/1'>disulfide bridge</scene>. Although the mechanism of disulfide bridge formation is still unknown, it is believed that <scene name='95/952714/Extracellular_glycosylation/1'>extracellular glycosylation</scene> via N-linked glycosylation (NAGs, shown in green) of various asparagine residues in the extracellular region of both the alpha and Ig beta chains help to facilitate this process. [https://en.wikipedia.org/wiki/Chaperone_(protein) Chaperon proteins] remain bound to the alpha and beta subunits until both dimerizations occur at which point the rest of the BCR complex can be recruited.

After Ig alpha/Ig beta dimerization the transmembrane helices of the heavy chains can embed within the B-cell membrane as well. The side chains of this <scene name='95/952714/Integral_helices/1'>4-pass integral helix structure </scene> are primarily hydrophobic side chains that allow for interactions with the hydrophobic tails in the [https://en.wikipedia.org/wiki/Lipid_bilayer phospholipid bilayer]. A total of 9 polar residues (picture that zooms in here??) between each of the heavy chains are included on the interior of the helix structure which interact with a few polar residues on the Ig alpha and Ig beta chains to hold the complex together. Additional interactions between the Ig alpha/Ig beta dimer and the heavy chains occur in the constant region.

===Constant Region===

Sandbox Reserved 1785: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 16: / Line 16: @@
 ===Transmembrane Region===
+The IgM BCR is tethered to [https://en.wikipedia.org/wiki/B_cell B-cell] membranes through the <scene name='95/952714/Integral_region/2'>transmembrane region </scene> which is broken up into both extracellular and integral domains. IgM BCR assembly requires dimerization of the <b><span class="text-brown">Ig alpha</span></b> and <b><span class="text-orange">Ig beta</span></b> subunits which embed within the B-cell membrane. The <scene name='95/952714/Ig_alpha_beta/1'> Ig alpha and beta heterodimer </scene> is dimerized in both the integral region, with a hydrogen bond, and within the extracellular region with a <scene name='95/952714/Extracellular_disulfide_bridge/1'>disulfide bridge</scene>. Although the mechanism of disulfide bridge formation is still unknown, it is believed that <scene name='95/952714/Extracellular_glycosylation/1'>extracellular glycosylation</scene> via N-linked glycosylation (NAGs, shown in green) of various asparagine residues in the extracellular region of both the <b><span class="text-brown">alpha</span></b> and <b><span class="text-orange">Ig beta</span></b> chains help to facilitate this process. [https://en.wikipedia.org/wiki/Chaperone_(protein) Chaperon proteins] remain bound to the alpha and beta subunits until both dimerizations occur at which point the rest of the BCR complex can be recruited.
+After <b><span class="text-brown">Ig alpha</span></b>/<b><span class="text-orange">Ig beta</span></b> dimerization the transmembrane helices of the heavy chains can embed within the B-cell membrane as well. The side chains of this <scene name='95/952714/Integral_helices/1'>4-pass integral helix structure </scene> are primarily hydrophobic side chains that allow for interactions with the hydrophobic tails in the [https://en.wikipedia.org/wiki/Lipid_bilayer phospholipid bilayer]. A total of 9 polar residues (picture that zooms in here??) between each of the heavy chains are included on the interior of the helix structure which interact with a few polar residues on the <b><span class="text-brown">Ig alpha</span></b> and <b><span class="text-orange">Ig beta</span></b> chains to hold the complex together. Additional interactions between the <b><span class="text-brown">Ig alpha</span></b>/<b><span class="text-orange">Ig beta</span></b> dimer and the heavy chains occur in the constant region.
 ===Constant Region===