Sandbox Reserved 1786: Difference between revisions

Line 34:

===Fc Region===

The constant region of IgM is made up of the two <scene name='95/952714/Heavy_chain/1'>heavy chains</scene>. These heavy chains form a bridge connecting the ~~FAB~~ region or variable region to the transmembrane region (Figure 1). They also act as a wire that the variable region can send a signal through to the transmembrane region as a mechanical change.

The constant region of IgM is made up of the two <scene name='95/952714/Heavy_chain/1'>heavy chains</scene>. These heavy chains form a bridge connecting the Fab region or variable region to the transmembrane region (Figure 1). They also act as a wire that the variable region can send a signal through to the transmembrane region as a mechanical change.

<scene name='95/952715/Extracellular_transmembrane_v2/10'>Extracellular transmembrane interactions</scene> help hold the heavy chains and Igα/Igβ chains together in the extracellular portion of the transmembrane region. Because a conformational change occurs throughout the entirety of the IgM-BCR complex, the Fc region must be able to tolerate the contortion of the structure as the antigen binds. In constant region two, which is located at the start of the Fc region, '''{{Font color|violet|heavy chain A}}''' and heavy chain B make a <scene name='95/952713/Disulfides/5'>disulfide bridge</scene> to stabilize the IgM-BCR and drive downstream signaling.

To maximize the Fc region’s signal transduction efficiency and Van der Waals contacts, constant region two of '''{{Font color|violet|heavy chain A}}''' makes an asymmetrical association with constant region three of heavy chain B to create a <scene name='95/952713/Trans_heavy/7'>heavy chain interface</scene>. More specifically, Arg243 and Arg251 residues from '''{{Font color|violet|heavy chain A}}''' donate three hydrogen bonds to Leu433, Thr431, and Asp376 residues on heavy chain B. Furthermore, Leu313 of heavy chain A accepts a hydrogen bond from Thr429 on heavy chain B. <ref name="Ma">PMID:35981028</ref>

To maximize the Fc region’s signal transduction efficiency and [https://en.wikipedia.org/wiki/Van_der_Waals_force#:~:text=If%20no%20other%20force%20is,between%20the%20atoms'%20electron%20clouds. Van der Waals contacts], constant region two of '''{{Font color|violet|heavy chain A}}''' makes an asymmetrical association with constant region three of heavy chain B to create a <scene name='95/952713/Trans_heavy/7'>heavy chain interface</scene>. More specifically, Arg243 and Arg251 residues from '''{{Font color|violet|heavy chain A}}''' donate three hydrogen bonds to Leu433, Thr431, and Asp376 residues on heavy chain B. Furthermore, Leu313 of heavy chain A accepts a hydrogen bond from Thr429 on heavy chain B. <ref name="Ma">PMID:35981028</ref>

----

Sandbox Reserved 1786: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 34: / Line 34: @@
 ===Fc Region===
-The constant region of IgM is made up of the two <scene name='95/952714/Heavy_chain/1'>heavy chains</scene>. These heavy chains form a bridge connecting the FAB region or variable region to the transmembrane region (Figure 1). They also act as a wire that the variable region can send a signal through to the transmembrane region as a mechanical change.
+The constant region of IgM is made up of the two <scene name='95/952714/Heavy_chain/1'>heavy chains</scene>. These heavy chains form a bridge connecting the Fab region or variable region to the transmembrane region (Figure 1). They also act as a wire that the variable region can send a signal through to the transmembrane region as a mechanical change.
 <scene name='95/952715/Extracellular_transmembrane_v2/10'>Extracellular transmembrane interactions</scene> help hold the heavy chains and <b><span class="text-brown">Igα</span></b>/<b><span class="text-orange">Igβ</span></b> chains together in the extracellular portion of the transmembrane region. Because a conformational change occurs throughout the entirety of the IgM-BCR complex, the Fc region must be able to tolerate the contortion of the structure as the antigen binds. In constant region two, which is located at the start of the Fc region, '''{{Font color|violet|heavy chain A}}''' and <b><span class="text-blue">heavy chain B</span></b> make a <scene name='95/952713/Disulfides/5'>disulfide bridge</scene> to stabilize the IgM-BCR and drive downstream signaling.
-To maximize the Fc region’s signal transduction efficiency and Van der Waals contacts, constant region two of '''{{Font color|violet|heavy chain A}}''' makes an asymmetrical association with constant region three of <b><span class="text-blue">heavy chain B</span></b> to create a <scene name='95/952713/Trans_heavy/7'>heavy chain interface</scene>. More specifically, Arg243 and Arg251 residues from '''{{Font color|violet|heavy chain A}}''' donate three hydrogen bonds to Leu433, Thr431, and Asp376 residues on <b><span class="text-blue">heavy chain B</span></b>. Furthermore, Leu313 of heavy chain A accepts a hydrogen bond from Thr429 on heavy chain B. <ref name="Ma">PMID:35981028</ref>
+To maximize the Fc region’s signal transduction efficiency and [https://en.wikipedia.org/wiki/Van_der_Waals_force#:~:text=If%20no%20other%20force%20is,between%20the%20atoms'%20electron%20clouds. Van der Waals contacts], constant region two of '''{{Font color|violet|heavy chain A}}''' makes an asymmetrical association with constant region three of <b><span class="text-blue">heavy chain B</span></b> to create a <scene name='95/952713/Trans_heavy/7'>heavy chain interface</scene>. More specifically, Arg243 and Arg251 residues from '''{{Font color|violet|heavy chain A}}''' donate three hydrogen bonds to Leu433, Thr431, and Asp376 residues on <b><span class="text-blue">heavy chain B</span></b>. Furthermore, Leu313 of heavy chain A accepts a hydrogen bond from Thr429 on heavy chain B. <ref name="Ma">PMID:35981028</ref>
 ----