Sandbox Reserved 1773: Difference between revisions

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===Antigen Binding Site===

[[Image:B cell diagram.jpg| 250 px| thumb|right|'''Figure 1.''' Overview of the human B Cell Receptor and its structural components. Used with permission under Wikimedia Commons.]]

The binding of an antigen to the human B Cell receptor is identical to other common soluble antibodies (such as [https://en.wikipedia.org/wiki/Immunoglobulin_G IgG], [https://en.wikipedia.org/wiki/Immunoglobulin_A IgA], [https://en.wikipedia.org/wiki/Immunoglobulin_M IgM], [https://en.wikipedia.org/wiki/Immunoglobulin_E IgE], or [https://en.wikipedia.org/wiki/Immunoglobulin_D IgD]). The antibody portion of the B Cell Receptor is roughly "Y" shaped and consists of two identical <scene name='95/952701/Heavy_chains_no_nag2_/2'>heavy</scene> and two identical <scene name='95/952701/Light_chains_highlight_no_nag2/2'>light</scene> chains creating two similar epitope binding regions<Ref name="Janeway CA">Janeway CA Jr, Travers P, Walport M, et al. Immunobiology: The Immune System in Health and Disease. 5th edition. New York: Garland Science; 2001. </Ref> (figure 1). Two antigen molecules can bind independent of one another to produce a response. Matching with standard FABs, the Ig portion has constant and variable region. The stem of the "Y" is a <scene name='95/952701/Constant_stem_no_nag/1'>constant region</scene> (<scene name='95/952701/Constant_zoom_no_nag/1'>constant region zoomed</scene>, [https://en.wikipedia.org/wiki/Antibody#CDRs,_Fv,_Fab_and_Fc_Regions Fc]) composed of only heavy chain interactions<Ref name="Janeway CA">Janeway CA Jr, Travers P, Walport M, et al. Immunobiology: The Immune System in Health and Disease. 5th edition. New York: Garland Science; 2001. </Ref>. The two heavy chains then branch at a flexible <scene name='95/952701/Hinge_no_nag/1'>hinge region</scene> (<scene name='95/952701/Hinge_no_nag_zoom/1'>hinge region zoomed</scene>). These interact individually with one light chain creating two [https://en.wikipedia.org/wiki/Antibody#CDRs,_Fv,_Fab_and_Fc_Regions Fab] fragments or branches of the "Y"<Ref name="Janeway CA">Janeway CA Jr, Travers P, Walport M, et al. Immunobiology: The Immune System in Health and Disease. 5th edition. New York: Garland Science; 2001. </Ref>. Light and heavy chains are held together via weak intermolecular forces and disulfide bridges<Ref name="Janeway CA">Janeway CA Jr, Travers P, Walport M, et al. Immunobiology: The Immune System in Health and Disease. 5th edition. New York: Garland Science; 2001 </Ref>. Each fab fragment (<scene name='95/952701/Fab_no_nag_zoom/1'>fab fragment zoomed</scene>) then terminates with two <scene name='95/952701/Fv_region/1'>variable regions</scene> ([https://en.wikipedia.org/wiki/Antibody#CDRs,_Fv,_Fab_and_Fc_Regions Fv]). These variable regions consist of hyper-variable loops, desired random coils of amino acids selected for specific recognition of a desired antigen <Ref name="Janeway CA">Janeway CA Jr, Travers P, Walport M, et al. Immunobiology: The Immune System in Health and Disease. 5th edition. New York: Garland Science; 2001. </Ref>. Binding to an antigen is determined based on intermolecular interactions to the hyper variable loops, and selectivity is provided by unique hyper variable loop sequences. Due to the identical structure of Fab fragments, BCR will recognize antigens in the same manner as do free antibodies. This is emphasized through Ma ''et al.'' who studied the IgG- BCR (VRC01) that targets gp120 of HIV-1 showing that the BCR form has an identical structure to the free antibody version (citation). This leads to a conformational change in the protein and transmits the signal through the membrane (citation).

The binding of an antigen to the human B Cell receptor is identical to other common soluble antibodies (such as [https://en.wikipedia.org/wiki/Immunoglobulin_G IgG], [https://en.wikipedia.org/wiki/Immunoglobulin_A IgA], [https://en.wikipedia.org/wiki/Immunoglobulin_M IgM], [https://en.wikipedia.org/wiki/Immunoglobulin_E IgE], or [https://en.wikipedia.org/wiki/Immunoglobulin_D IgD]). The antibody portion of the B Cell Receptor is roughly "Y" shaped and consists of two identical <scene name='95/952701/Heavy_chains_no_nag2_/2'>heavy</scene> and two identical <scene name='95/952701/Light_chains_highlight_no_nag2/2'>light</scene> chains creating two similar epitope binding regions<Ref name="Janeway CA">Janeway CA Jr, Travers P, Walport M, et al. Immunobiology: The Immune System in Health and Disease. 5th edition. New York: Garland Science; 2001. </Ref> (figure 1). Two antigen molecules can bind independent of one another to produce a response. Matching with standard FABs, the Ig portion has constant and variable region. The stem of the "Y" is a <scene name='95/952701/Constant_stem_no_nag/1'>constant region</scene> (<scene name='95/952701/Constant_zoom_no_nag/1'>constant region zoomed</scene>, [https://en.wikipedia.org/wiki/Antibody#CDRs,_Fv,_Fab_and_Fc_Regions Fc]) composed of only heavy chain interactions<Ref name="Janeway CA">Janeway CA Jr, Travers P, Walport M, et al. Immunobiology: The Immune System in Health and Disease. 5th edition. New York: Garland Science; 2001. </Ref>. The two heavy chains then branch at a flexible <scene name='95/952701/Hinge_no_nag/1'>hinge region</scene> (<scene name='95/952701/Hinge_no_nag_zoom/1'>hinge region zoomed</scene>). These interact individually with one light chain creating two [https://en.wikipedia.org/wiki/Antibody#CDRs,_Fv,_Fab_and_Fc_Regions Fab] fragments or branches of the "Y"<Ref name="Janeway CA">Janeway CA Jr, Travers P, Walport M, et al. Immunobiology: The Immune System in Health and Disease. 5th edition. New York: Garland Science; 2001. </Ref>. Light and heavy chains are held together via weak intermolecular forces and disulfide bridges<Ref name="Janeway CA">Janeway CA Jr, Travers P, Walport M, et al. Immunobiology: The Immune System in Health and Disease. 5th edition. New York: Garland Science; 2001 </Ref>. Each <scene name='95/952701/Fab_no_nag/1'>fab fragment</scene> (<scene name='95/952701/Fab_no_nag_zoom/1'>fab fragment zoomed</scene>) then terminates with two <scene name='95/952701/Fv_region/1'>variable regions</scene> ([https://en.wikipedia.org/wiki/Antibody#CDRs,_Fv,_Fab_and_Fc_Regions Fv]). These variable regions consist of hyper-variable loops, desired random coils of amino acids selected for specific recognition of a desired antigen <Ref name="Janeway CA">Janeway CA Jr, Travers P, Walport M, et al. Immunobiology: The Immune System in Health and Disease. 5th edition. New York: Garland Science; 2001. </Ref>. Binding to an antigen is determined based on intermolecular interactions to the hyper variable loops, and selectivity is provided by unique hyper variable loop sequences. Due to the identical structure of Fab fragments, BCR will recognize antigens in the same manner as do free antibodies. This is emphasized through Ma ''et al.'' who studied the IgG- BCR (VRC01) that targets gp120 of HIV-1 showing that the BCR form has an identical structure to the free antibody version (citation). This leads to a conformational change in the protein and transmits the signal through the membrane (citation).

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@@ Line 14: / Line 14: @@
 ===Antigen Binding Site===
 [[Image:B cell diagram.jpg| 250 px| thumb|right|'''Figure 1.''' Overview of the human B Cell Receptor and its structural components. Used with permission under Wikimedia Commons.]]
-The binding of an antigen to the human B Cell receptor is identical to other common soluble antibodies (such as [https://en.wikipedia.org/wiki/Immunoglobulin_G IgG], [https://en.wikipedia.org/wiki/Immunoglobulin_A IgA], [https://en.wikipedia.org/wiki/Immunoglobulin_M IgM], [https://en.wikipedia.org/wiki/Immunoglobulin_E IgE], or [https://en.wikipedia.org/wiki/Immunoglobulin_D IgD]). The antibody portion of the B Cell Receptor is roughly "Y" shaped and consists of two identical <scene name='95/952701/Heavy_chains_no_nag2_/2'>heavy</scene> and two identical <scene name='95/952701/Light_chains_highlight_no_nag2/2'>light</scene> chains creating two similar epitope binding regions<Ref name="Janeway CA">Janeway CA Jr, Travers P, Walport M, et al. Immunobiology: The Immune System in Health and Disease. 5th edition. New York: Garland Science; 2001. </Ref> (figure 1). Two antigen molecules can bind independent of one another to produce a response. Matching with standard FABs, the Ig portion has constant and variable region. The stem of the "Y" is a <scene name='95/952701/Constant_stem_no_nag/1'>constant region</scene> (<scene name='95/952701/Constant_zoom_no_nag/1'>constant region zoomed</scene>, [https://en.wikipedia.org/wiki/Antibody#CDRs,_Fv,_Fab_and_Fc_Regions Fc]) composed of only heavy chain interactions<Ref name="Janeway CA">Janeway CA Jr, Travers P, Walport M, et al. Immunobiology: The Immune System in Health and Disease. 5th edition. New York: Garland Science; 2001. </Ref>. The two heavy chains then branch at a flexible <scene name='95/952701/Hinge_no_nag/1'>hinge region</scene> (<scene name='95/952701/Hinge_no_nag_zoom/1'>hinge region zoomed</scene>). These interact individually with one light chain creating two [https://en.wikipedia.org/wiki/Antibody#CDRs,_Fv,_Fab_and_Fc_Regions Fab] fragments or branches of the "Y"<Ref name="Janeway CA">Janeway CA Jr, Travers P, Walport M, et al. Immunobiology: The Immune System in Health and Disease. 5th edition. New York: Garland Science; 2001. </Ref>. Light and heavy chains are held together via weak intermolecular forces and disulfide bridges<Ref name="Janeway CA">Janeway CA Jr, Travers P, Walport M, et al. Immunobiology: The Immune System in Health and Disease. 5th edition. New York: Garland Science; 2001 </Ref>. Each fab fragment (<scene name='95/952701/Fab_no_nag_zoom/1'>fab fragment zoomed</scene>) then terminates with two <scene name='95/952701/Fv_region/1'>variable regions</scene> ([https://en.wikipedia.org/wiki/Antibody#CDRs,_Fv,_Fab_and_Fc_Regions Fv]). These variable regions consist of hyper-variable loops, desired random coils of amino acids selected for specific recognition of a desired antigen <Ref name="Janeway CA">Janeway CA Jr, Travers P, Walport M, et al. Immunobiology: The Immune System in Health and Disease. 5th edition. New York: Garland Science; 2001. </Ref>. Binding to an antigen is determined based on intermolecular interactions to the hyper variable loops, and selectivity is provided by unique hyper variable loop sequences. Due to the identical structure of Fab fragments, BCR will recognize antigens in the same manner as do free antibodies. This is emphasized through Ma ''et al.'' who studied the IgG- BCR (VRC01) that targets gp120 of HIV-1 showing that the BCR form has an identical structure to the free antibody version (citation). This leads to a conformational change in the protein and transmits the signal through the membrane (citation).
+The binding of an antigen to the human B Cell receptor is identical to other common soluble antibodies (such as [https://en.wikipedia.org/wiki/Immunoglobulin_G IgG], [https://en.wikipedia.org/wiki/Immunoglobulin_A IgA], [https://en.wikipedia.org/wiki/Immunoglobulin_M IgM], [https://en.wikipedia.org/wiki/Immunoglobulin_E IgE], or [https://en.wikipedia.org/wiki/Immunoglobulin_D IgD]). The antibody portion of the B Cell Receptor is roughly "Y" shaped and consists of two identical <scene name='95/952701/Heavy_chains_no_nag2_/2'>heavy</scene> and two identical <scene name='95/952701/Light_chains_highlight_no_nag2/2'>light</scene> chains creating two similar epitope binding regions<Ref name="Janeway CA">Janeway CA Jr, Travers P, Walport M, et al. Immunobiology: The Immune System in Health and Disease. 5th edition. New York: Garland Science; 2001. </Ref> (figure 1). Two antigen molecules can bind independent of one another to produce a response. Matching with standard FABs, the Ig portion has constant and variable region. The stem of the "Y" is a <scene name='95/952701/Constant_stem_no_nag/1'>constant region</scene> (<scene name='95/952701/Constant_zoom_no_nag/1'>constant region zoomed</scene>, [https://en.wikipedia.org/wiki/Antibody#CDRs,_Fv,_Fab_and_Fc_Regions Fc]) composed of only heavy chain interactions<Ref name="Janeway CA">Janeway CA Jr, Travers P, Walport M, et al. Immunobiology: The Immune System in Health and Disease. 5th edition. New York: Garland Science; 2001. </Ref>. The two heavy chains then branch at a flexible <scene name='95/952701/Hinge_no_nag/1'>hinge region</scene> (<scene name='95/952701/Hinge_no_nag_zoom/1'>hinge region zoomed</scene>). These interact individually with one light chain creating two [https://en.wikipedia.org/wiki/Antibody#CDRs,_Fv,_Fab_and_Fc_Regions Fab] fragments or branches of the "Y"<Ref name="Janeway CA">Janeway CA Jr, Travers P, Walport M, et al. Immunobiology: The Immune System in Health and Disease. 5th edition. New York: Garland Science; 2001. </Ref>. Light and heavy chains are held together via weak intermolecular forces and disulfide bridges<Ref name="Janeway CA">Janeway CA Jr, Travers P, Walport M, et al. Immunobiology: The Immune System in Health and Disease. 5th edition. New York: Garland Science; 2001 </Ref>. Each <scene name='95/952701/Fab_no_nag/1'>fab fragment</scene> (<scene name='95/952701/Fab_no_nag_zoom/1'>fab fragment zoomed</scene>) then terminates with two <scene name='95/952701/Fv_region/1'>variable regions</scene> ([https://en.wikipedia.org/wiki/Antibody#CDRs,_Fv,_Fab_and_Fc_Regions Fv]). These variable regions consist of hyper-variable loops, desired random coils of amino acids selected for specific recognition of a desired antigen <Ref name="Janeway CA">Janeway CA Jr, Travers P, Walport M, et al. Immunobiology: The Immune System in Health and Disease. 5th edition. New York: Garland Science; 2001. </Ref>. Binding to an antigen is determined based on intermolecular interactions to the hyper variable loops, and selectivity is provided by unique hyper variable loop sequences. Due to the identical structure of Fab fragments, BCR will recognize antigens in the same manner as do free antibodies. This is emphasized through Ma ''et al.'' who studied the IgG- BCR (VRC01) that targets gp120 of HIV-1 showing that the BCR form has an identical structure to the free antibody version (citation). This leads to a conformational change in the protein and transmits the signal through the membrane (citation).