Sandbox Reserved 1771: Difference between revisions

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==Function==

Once bound to an antigen, BCRs undergo a conformational change in the extracellular region. While the exact conformational change is still not known, preliminary studies suggest that there is separation of Fab fragments that opens the binding site within the BCR(ref). This initiates several signal transduction pathways, which are responsible for processing the antigen and initiating the appropriate immune responses. More specifically, the α-β subunit is connected to the phosphorylation of an [https://en.wikipedia.org/wiki/Immunoreceptor_tyrosine-based_activation_motif immunoreceptor tyrosine-based activation motif](ITAM) upon binding. This in turn triggers the activation of kinases downstream that aid in the immune response. BCRs can be oligomeric prior to antigen binding, but once bound become an active monomer.

Once bound to an antigen, BCRs undergo a conformational change in the extracellular region. While the exact conformational change is still not known, preliminary studies suggest that there is separation of Fab fragments that opens the binding site within the BCR(ref). This initiates several signal transduction pathways, which are responsible for processing the antigen and initiating the appropriate immune responses. More specifically, the α-β subunit is connected to the phosphorylation of an [https://en.wikipedia.org/wiki/Immunoreceptor_tyrosine-based_activation_motif immunoreceptor tyrosine-based activation motif](ITAM) upon binding. This in turn triggers the activation of kinases downstream that aid in the immune response. BCRs can be oligomeric prior to antigen binding, but once bound become an active monomer. <Ref name="ShenSichen Z"> ShenSichen Z, LiZhengpeng L, Liu W,(2019) Conformational change within the extracellular domain of B cell receptor in B cell activation upon antigen binding [eLife 8:e42271. https://doi.org/10.7554/eLife.42271]</Ref>.

==Medical Relevancy==

Sandbox Reserved 1771: Difference between revisions

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 ==Function==
-Once bound to an antigen, BCRs undergo a conformational change in the extracellular region. While the exact conformational change is still not known, preliminary studies suggest that there is separation of Fab fragments that opens the binding site within the BCR(ref). This initiates several signal transduction pathways, which are responsible for processing the antigen and initiating the appropriate immune responses. More specifically, the α-β subunit is connected to the phosphorylation of an [https://en.wikipedia.org/wiki/Immunoreceptor_tyrosine-based_activation_motif immunoreceptor tyrosine-based activation motif](ITAM) upon binding. This in turn triggers the activation of kinases downstream that aid in the immune response. BCRs can be oligomeric prior to antigen binding, but once bound become an active monomer.
+Once bound to an antigen, BCRs undergo a conformational change in the extracellular region. While the exact conformational change is still not known, preliminary studies suggest that there is separation of Fab fragments that opens the binding site within the BCR(ref). This initiates several signal transduction pathways, which are responsible for processing the antigen and initiating the appropriate immune responses. More specifically, the α-β subunit is connected to the phosphorylation of an [https://en.wikipedia.org/wiki/Immunoreceptor_tyrosine-based_activation_motif immunoreceptor tyrosine-based activation motif](ITAM) upon binding. This in turn triggers the activation of kinases downstream that aid in the immune response. BCRs can be oligomeric prior to antigen binding, but once bound become an active monomer.  <Ref name="ShenSichen Z"> ShenSichen Z, LiZhengpeng L, Liu W,(2019) Conformational change within the extracellular domain of B cell receptor in B cell activation upon antigen binding [eLife 8:e42271. https://doi.org/10.7554/eLife.42271]</Ref>.
 ==Medical Relevancy==