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Junctional diversity refers to the variability introduced at the junctions between V, D, and J gene segments during TCR gene rearrangement.
True
Non-germline sequences in the TCR variable regions result from the duplication of nucleotides in the CDR3 region.
False
The domain structure of TCR proteins includes variable, constant, transmembrane, and cytoplasmic domains in both the alpha and gamma chains.
False
N/P nucleotides are non-germline sequences added to segment junctions during gene rearrangement.
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Diverse antigen receptor genes from the same germline DNA are generated by random V + random D + random J recombination.
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V(D)J recombination is a process that only occurs in mature B cells.
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The diversity generated by V(D)J recombination in lymphocytes is essential for recognizing only specific antigens.
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Complementarity-determining regions (CDRs) are introduced during germline organization of the human immunoglobulin heavy chain locus.
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Non-Germline Sequences play a significant role in the structure of T cell receptors.
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The domain structure of immunoglobulin (Ig) proteins includes only V (Variable) and C (Constant) regions.
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The diversity of CDR3 in TCRs allows them to recognize and bind specific peptide antigens presented by MHC molecules.
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Similar to Ig proteins, TCRs do not contain constant domains that determine their effector functions and structural characteristics.
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The constant regions of TCR chains are not responsible for mediating intracellular signaling upon antigen recognition and binding.
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The germline organization of human TCR alpha and beta chains does not involve V(D)J recombination and junctional diversity.
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The domain structure of T cell receptor (TCR) proteins includes multiple domains in the alpha chain such as variable (V), constant (C), transmembrane (TM), and cytoplasmic (CYTO) domains.
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During V(D)J recombination, non-germline sequences are introduced at the junctions between V, D, and J gene segments, particularly in CDR2.
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The enzyme terminal deoxynucleotidyl transferase (TdT) removes nucleotides during the recombination process.
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Non-germline sequences in CDR3 are irrelevant to the diversity and specificity of recognizing peptide antigens presented by MHC molecules.
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The variability of CDR3 sequences, including non-germline sequences, hinders Ig proteins from recognizing a wide range of antigens with high specificity.
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The germline organization of human TCR α and β chains does not share similar principles with the immunoglobulin (Ig) heavy chain in terms of their genetic organization and diversity generation.
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During T cell development, precursor cells undergo random rearrangement of V, D, and J gene segments to form functional TCR genes.
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The junctions between rearranged V, D, and J gene segments in TCRs cannot undergo addition or deletion of nucleotides.
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The complementarity-determining region 3 (CDR3) in TCRs is not important for antigen recognition.
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The germline organization of TCR genes includes multiple V, D (only in TCR β chains), and J gene segments arranged in a random order along the chromosome.
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The process of V(D)J recombination in TCRs generates limited diversity in their variable regions compared to Ig heavy chains.
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The TM domain encoded by the C gene ensures that the antibody molecule remains associated with the T cell membrane.
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The CYTO domain transduces signals from the BCR upon antigen binding, leading to B cell activation, proliferation, and differentiation.
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The V, D, and J segments contribute to the constant region structure of the antibody molecule.
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The domain structure of immunoglobulin proteins is not essential for their function and diversity.
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The CDR3 plays a significant role in the domain structure of Ig proteins.
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Each heavy and light chain of Ig proteins is composed of multiple constant domains
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CDRs are loops within the constant domains of Ig proteins
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There are five CDRs in each variable domain: CDR1, CDR2, CDR3, CDR4, and CDR5
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CDR3 is the least diverse region among antibodies, TCRs, and B cell receptors
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The diversity of CDR3 arises from the specific recombination of gene segments during the rearrangement process
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The high diversity of CDR3 sequences limits the ability of Ig proteins to recognize a vast array of antigens with specificity
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The unique sequence of CDR3 has no effect on the antigen-binding affinity of Ig proteins
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Junctional diversity refers to the variability introduced at the junctions between V, D, and J gene segments during B cell receptor gene rearrangement
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Complementarity-determining regions (CDRs) are introduced during somatic hypermutation of the human immunoglobulin heavy chain locus
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Non-germline sequences in TCR variable regions result from the duplication of nucleotides in the CDR3 region
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