Sandbox Reserved 1786: Difference between revisions
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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 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; this allows for interactions with the hydrophobic tails in the [https://en.wikipedia.org/wiki/Lipid_bilayer phospholipid bilayer]. The four helices (Figure 2) are intertwined and primarily held together through interactions between the <scene name='95/952714/Integral_helices_2/3'>hydrophobic side chains</scene>; however, a a few polar residues are included which allow for additional interactions with the 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"/> | 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 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; this allows for interactions with the hydrophobic tails in the [https://en.wikipedia.org/wiki/Lipid_bilayer phospholipid bilayer]. The four helices (Figure 2) are intertwined and primarily held together through interactions between the <scene name='95/952714/Integral_helices_2/3'>hydrophobic side chains</scene>; however, a a few polar residues are included which allow for additional interactions with the 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"/> | ||
[[Image:Integral_helix_figure.png|400 px|left|thumb|'''Figure 2. 4-pass integral helix.''' PyMOL image of the integral helices in IgM BCR (PDB:7xq8) rotated on the x and y axes. Side chains are shown as sticks. Brown=Ig alpha, orange=Ig beta, pink=heavy chain A, blue=heavy chain B.]] | [[Image:Integral_helix_figure.png|400 px|left|thumb|'''Figure 2. 4-pass integral helix.''' PyMOL image of the integral helices in IgM BCR (PDB:7xq8). The structure is shown rotated on the x and y axes to illustrate how the chains are intertwined. Side chains are shown as sticks. Brown=Ig alpha, orange=Ig beta, pink=heavy chain A, blue=heavy chain B.]] | ||
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