Sandbox Reserved 1786: Difference between revisions

Line 17:

===Transmembrane Region===

The IgM BCR is anchored to [https://en.wikipedia.org/wiki/B_cell B-cell] membranes through the <scene name='95/952714/Integral_region/15'>transmembrane region</scene> which is broken up into both extracellular and integral domains which sit on top of or span through the membrane, respectively (Figure 1). IgM BCR assembly requires dimerization of the Igα and Igβ subunits which embed within the B-cell membrane. <ref name="Tolar"/> The <scene name='95/952714/Ig_alpha_beta/5'>Igα and Igβ heterodimer</scene> dimerizes within the extracellular region with a <scene name='95/952714/Extracellular_disulfide_bridge/6'>disulfide bridge</scene>. Additional dimerization occurs within the integral region via a hydrogen bond; the residues involved have not been confirmed. Although the mechanism of disulfide bridge formation is still unknown, <scene name='95/952714/Extracellular_glycosylation/2'>extracellular glycosylation</scene> via [https://en.wikipedia.org/wiki/N-linked_glycosylation N-linked asparagine glycosyl groups] (NAGs) on various residues in the extracellular region of both the Igα and and Igβ chains is hypothesized to ~~help~~ facilitate this process by recruiting [https://en.wikipedia.org/wiki/Chaperone_(protein) Chaperone proteins] to optimize the folding process. <ref name="Daniels">PMID:12535523</ref> Past studies with human and viral proteins have shown that the presence of NAGs not only facilitate the rapid formation of disulfide bridges, but also ensure correct location. <ref name="Bakshi">PMID:35409101</ref>, <ref name="Mirazimi">PMID:9557673</ref> The recruited chaperone proteins will typically remain bound to the Igα and Igβ subunits until dimerization occurs. <ref name="Dylke"/>

The IgM BCR is anchored to [https://en.wikipedia.org/wiki/B_cell B-cell] membranes through the <scene name='95/952714/Integral_region/15'>transmembrane region</scene> which is broken up into both extracellular and integral domains which sit on top of or span through the membrane, respectively (Figure 1). IgM BCR assembly requires dimerization of the Igα and Igβ subunits which embed within the B-cell membrane. <ref name="Tolar"/> The <scene name='95/952714/Ig_alpha_beta/5'>Igα and Igβ heterodimer</scene> dimerizes within the extracellular region with a <scene name='95/952714/Extracellular_disulfide_bridge/6'>disulfide bridge</scene>. Additional dimerization occurs within the integral region via a hydrogen bond; the residues involved have not been confirmed. Although the mechanism of disulfide bridge formation is still unknown, <scene name='95/952714/Extracellular_glycosylation/2'>extracellular glycosylation</scene> via [https://en.wikipedia.org/wiki/N-linked_glycosylation N-linked asparagine glycosyl groups] (NAGs) on various residues in the extracellular region of both the Igα and and Igβ chains is hypothesized to facilitate this process by recruiting [https://en.wikipedia.org/wiki/Chaperone_(protein) Chaperone proteins] to optimize the folding process. <ref name="Daniels">PMID:12535523</ref> Past studies with human and viral proteins have shown that the presence of NAGs not only facilitate the rapid formation of disulfide bridges, but also ensure correct location. <ref name="Bakshi">PMID:35409101</ref>, <ref name="Mirazimi">PMID:9557673</ref> The recruited chaperone proteins will typically remain bound to the Igα and Igβ subunits until dimerization occurs. <ref name="Dylke"/>

After Igα and Igβ dimerization, the transmembrane helices of the heavy chains can embed within the B-cell membrane and will intertwine with the Igα and Igβ chains. <ref name="Tolar"/> The side chains of this <scene name='95/952714/Integral_helices_2/2'>4-pass integral helix structure</scene>, made up by the alpha, beta, and heavy chains ('''{{Font color|violet|A}}'''/B), are primarily hydrophobic side chains that allow for interactions with the hydrophobic tails in the [https://en.wikipedia.org/wiki/Lipid_bilayer phospholipid bilayer]. The four helices (Figure 2) are primarily held together through hydrophobic interactions; however, a a few polar residues are included on the interior of the helix structure which interact with a few polar residues on the Igα and Igβ chains. <ref name="Dylke"/>

@@ Line 17: / Line 17: @@
 ===Transmembrane Region===
-The IgM BCR is anchored to [https://en.wikipedia.org/wiki/B_cell B-cell] membranes through the <scene name='95/952714/Integral_region/15'>transmembrane region</scene> which is broken up into both extracellular and integral domains which sit on top of or span through the membrane, respectively (Figure 1). IgM BCR assembly requires dimerization of the <b><span class="text-brown">Igα</span></b> and <b><span class="text-orange">Igβ</span></b> subunits which embed within the B-cell membrane. <ref name="Tolar"/> The <scene name='95/952714/Ig_alpha_beta/5'>Igα and Igβ heterodimer</scene> dimerizes within the extracellular region with a <scene name='95/952714/Extracellular_disulfide_bridge/6'>disulfide bridge</scene>. Additional dimerization occurs within the integral region via a hydrogen bond; the residues involved have not been confirmed. Although the mechanism of disulfide bridge formation is still unknown, <scene name='95/952714/Extracellular_glycosylation/2'>extracellular glycosylation</scene> via [https://en.wikipedia.org/wiki/N-linked_glycosylation N-linked asparagine glycosyl groups] <b><span class="text-lightgreen">(NAGs)</span></b> on various residues in the extracellular region of both the <b><span class="text-brown">Igα</span></b> and and <b><span class="text-orange">Igβ</span></b> chains is hypothesized to help facilitate this process by recruiting [https://en.wikipedia.org/wiki/Chaperone_(protein) Chaperone proteins] to optimize the folding process. <ref name="Daniels">PMID:12535523</ref> Past studies with human and viral proteins have shown that the presence of NAGs not only facilitate the rapid formation of disulfide bridges, but also ensure correct location. <ref name="Bakshi">PMID:35409101</ref>, <ref name="Mirazimi">PMID:9557673</ref> The recruited chaperone proteins will typically remain bound to the <b><span class="text-brown">Igα</span></b> and <b><span class="text-orange">Igβ</span></b> subunits until dimerization occurs. <ref name="Dylke"/>
+The IgM BCR is anchored to [https://en.wikipedia.org/wiki/B_cell B-cell] membranes through the <scene name='95/952714/Integral_region/15'>transmembrane region</scene> which is broken up into both extracellular and integral domains which sit on top of or span through the membrane, respectively (Figure 1). IgM BCR assembly requires dimerization of the <b><span class="text-brown">Igα</span></b> and <b><span class="text-orange">Igβ</span></b> subunits which embed within the B-cell membrane. <ref name="Tolar"/> The <scene name='95/952714/Ig_alpha_beta/5'>Igα and Igβ heterodimer</scene> dimerizes within the extracellular region with a <scene name='95/952714/Extracellular_disulfide_bridge/6'>disulfide bridge</scene>. Additional dimerization occurs within the integral region via a hydrogen bond; the residues involved have not been confirmed. Although the mechanism of disulfide bridge formation is still unknown, <scene name='95/952714/Extracellular_glycosylation/2'>extracellular glycosylation</scene> via [https://en.wikipedia.org/wiki/N-linked_glycosylation N-linked asparagine glycosyl groups] <b><span class="text-lightgreen">(NAGs)</span></b> on various residues in the extracellular region of both the <b><span class="text-brown">Igα</span></b> and and <b><span class="text-orange">Igβ</span></b> chains is hypothesized to facilitate this process by recruiting [https://en.wikipedia.org/wiki/Chaperone_(protein) Chaperone proteins] to optimize the folding process. <ref name="Daniels">PMID:12535523</ref> Past studies with human and viral proteins have shown that the presence of NAGs not only facilitate the rapid formation of disulfide bridges, but also ensure correct location. <ref name="Bakshi">PMID:35409101</ref>, <ref name="Mirazimi">PMID:9557673</ref> The recruited chaperone proteins will typically remain bound to the <b><span class="text-brown">Igα</span></b> and <b><span class="text-orange">Igβ</span></b> subunits until dimerization occurs. <ref name="Dylke"/>
 After <b><span class="text-brown">Igα</span></b> and <b><span class="text-orange">Igβ</span></b> dimerization, the transmembrane helices of the heavy chains can embed within the B-cell membrane and will intertwine with the <b><span class="text-brown">Igα</span></b> and <b><span class="text-orange">Igβ</span></b> chains. <ref name="Tolar"/> The side chains of this <scene name='95/952714/Integral_helices_2/2'>4-pass integral helix structure</scene>, made up by the <b><span class="text-brown">alpha</span></b>, <b><span class="text-orange">beta</span></b>, and heavy chains ('''{{Font color|violet|A}}'''/<b><span class="text-blue">B</span></b>), are primarily hydrophobic side chains that allow for interactions with the hydrophobic tails in the [https://en.wikipedia.org/wiki/Lipid_bilayer phospholipid bilayer]. The four helices (Figure 2) are primarily held together through hydrophobic interactions; however, a a few polar residues are included on the interior of the helix structure which interact with a few polar residues on the <b><span class="text-brown">Igα</span></b> and <b><span class="text-orange">Igβ</span></b> chains. <ref name="Dylke"/>

Sandbox Reserved 1786: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools