Microbiology and Immunology 3300B Lecture Notes - Lecture 7: B-Cell Receptor, Clonal Selection, Immunoglobulin Light Chain
22 Nov 2012
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How does an immune system that is evolutionarily conserved and slow to change. Respond to pathogens that can evolve rapidly: nature has come up with an inventive, effective, but also dangerous solution to this problem, b cell receptors, t cell receptors, and antibodies function as adaptor molecules. B cell receptors and antibodies consist of four. Polypeptide chains linked by disulphide bonds: light chains: , , , , or : antibody types are defined by heavy chains. Immunoglobulin heavy and light chains are composed of. Antibody molecules can be cleaved into functionally distinct fragments. Pepsin: fab: fragment antigen binding , fc: fragment crystallizable . The domains of an immunoglobulin molecule are structurally similar. Ig genes are rearranged at the dna level. In antibody-producing cells: discovered by hozumi and tonegawa (nobel prize, 1987, proteins rag-1 and rag-2 function together as a. V(d)j recombinase: rag proteins recognize and cut dna at recombination signal sequences (rsss, dna sequences are repaired by dna repair pathways.
