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Sandbox Reserved 1786

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===Transmembrane Region===
===Transmembrane Region===
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The IgM BCR is tethered to 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. Embedding within the BCR membrane are the <scene name='95/952714/Integral_helices/1'>4-pass integral helices</scene>. Each of these helices are composed primarily of hydrophobic side chains that allow for interactions with the hydrophobic tails in the phospholipid bilayer.
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The IgM BCR is tethered to 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 (brown and orange chains) 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'>glycosylation of various asparagine residues</scene> in the extracellular region of both the alpha and beta chains help to facilitate this process. Thes NAG glycosyl structures are include in this structure colored green. Chaperone 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.
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<scene name='95/952714/Ig_alpha_beta/1'>Ig alpha and beta subunits form a heterodimer </scene>
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After alpha/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 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 alpha and beta chains to hold the complex together. Additional interactions between the alpha/beta dimer and the heavy chains occur in the constant region.
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<scene name='95/952714/Extracellular_disulfide_bridge/1'>extracellular disulfide bridge</scene>
 
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<scene name='95/952714/Extracellular_glycosylation/1'>extracellular glycosylation</scene>
 
===Constant Region===
===Constant Region===

Revision as of 16:36, 31 March 2023

This Sandbox is Reserved from February 27 through August 31, 2023 for use in the course CH462 Biochemistry II taught by R. Jeremy Johnson at the Butler University, Indianapolis, USA. This reservation includes Sandbox Reserved 1765 through Sandbox Reserved 1795.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
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More help: Help:Editing

Human B-cell Antigen Receptor: IgM BCR

IgM B-Cell Receptor (PDB: 7xq8)

Drag the structure with the mouse to rotate

References


Student Contributors

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