Final answer:
T-cell receptors are similar to immunoglobulins in the sense that both have variable regions with complementarity-determining regions and exhibit extensive repertoire diversity. However, TCRs are always membrane-bound and do not undergo affinity maturation through somatic hypermutation like immunoglobulins do.
Step-by-step explanation:
Ways in which T-cell receptors (TCRs) are similar to immunoglobulins include having a variable region that contains a set of complementarity-determining regions (CDRs) that determine antigen specificity, and both exhibit a vast diversity in their repertoire. Specifically, the TCR variable region contains three CDRs encoded by the Vα domain and three CDRs encoded by the Vβ domain, similar to the CDRs encoded by the variable heavy (VH) and variable light (VL) domains in immunoglobulins. Additionally, there is immense diversity in the TCR repertoire due to the mutation and recombination of gene segments in stem cell precursors of T cells, akin to the diversity generation in the B-cell receptor (BCR) and immunoglobulin repertoire.
However, T-cell receptors differ from immunoglobulins in several key aspects. Unlike immunoglobulins, TCRs are not found in a secreted form; they are only membrane-bound. Moreover, TCRs do not undergo affinity maturation through somatic hypermutation post antigen-binding, which is a characteristic process for immunoglobulins.