Sandbox Reserved 1771: Difference between revisions
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==Structure== | ==Structure== | ||
B cell receptors have distinct functional domains each playing a unique role in response to a foreign antigen. These include the extracellular domain, the transmembrane domain, and the intracellular domain (the structure of this domain is still unclear). To accomplish B cell signaling, the BCR must bind an antigen and transmit the signal through the receptor domains. Exploring the different sections of a BCR, the antigen binding site (located in the extracellular region) is specific to antigens, but the process is highly conserved across different BCRs. More specifically, the IgM BCR has a unique interaction concerning its Fc chains and a/b subunits. These interactions contribute to the overall structure of the protein. This section will explore these structural regions starting with the extracellular domain, describing the antigen binding domain, outlining unique interactions between Fc chains and a/b subunits, and describing the intermolecular interactions that keep subunits together. Ultimately, the interactions of the transmembrane domain that anchor the complex to the membrane are examined. | B cell receptors have distinct functional domains each playing a unique role in response to a foreign antigen. These include the extracellular domain, the transmembrane domain, and the intracellular domain (the structure of this domain is still unclear).<Ref name="Su Q"> Su Q, Chen M, Shi Y, Zhang X, Huang G, Huang B, Liu D, Liu Z, Shi Y. Cryo-EM structure of the human IgM B cell receptor. Science. 2022 Aug 19;377(6608):875-880. [doi: 10.1126/science.abo3923. Epub 2022 Aug 18. PMID: 35981043.]</Ref> To accomplish B cell signaling, the BCR must bind an antigen and transmit the signal through the receptor domains. Exploring the different sections of a BCR, the antigen binding site (located in the extracellular region) is specific to antigens, but the process is highly conserved across different BCRs.<Ref name="Su Q"> Su Q, Chen M, Shi Y, Zhang X, Huang G, Huang B, Liu D, Liu Z, Shi Y. Cryo-EM structure of the human IgM B cell receptor. Science. 2022 Aug 19;377(6608):875-880. [doi: 10.1126/science.abo3923. Epub 2022 Aug 18. PMID: 35981043.]</Ref> More specifically, the IgM BCR has a unique interaction concerning its Fc chains and a/b subunits.<Ref name="Su Q"> Su Q, Chen M, Shi Y, Zhang X, Huang G, Huang B, Liu D, Liu Z, Shi Y. Cryo-EM structure of the human IgM B cell receptor. Science. 2022 Aug 19;377(6608):875-880. [doi: 10.1126/science.abo3923. Epub 2022 Aug 18. PMID: 35981043.]</Ref> These interactions contribute to the overall structure of the protein. This section will explore these structural regions starting with the extracellular domain, describing the antigen binding domain, outlining unique interactions between Fc chains and a/b subunits, and describing the intermolecular interactions that keep subunits together. Ultimately, the interactions of the transmembrane domain that anchor the complex to the membrane are examined. | ||
===Antigen Binding Site=== | ===Antigen Binding Site=== | ||