PDZ domains are common structural domains found in signaling proteins across various species, including bacteria, yeast, plants, viruses, and animals . These domains are typically composed of 80-90 amino acids and play a crucial role in anchoring receptor proteins in the membrane to cytoskeletal components . PDZ domains are named after the first three proteins discovered to share this domain: post-synaptic density protein (PSD95), Drosophila disc large tumor suppressor (Dlg1), and zonula occludens-1 protein (zo-1) .
PDZ domains are small, modular entities consisting of 5 or 6 β-strands and 2 or 3 α-helical structures . They typically recognize the extreme C-termini of target proteins, but some also recognize internal sequence motifs through a single binding site on the domains . These domains are involved in various biological processes, including transport, ion channel signaling, and other signal transduction systems .
PDZ Domain Containing 11 (PDZD11) is a protein-coding gene associated with several diseases, including Non-Syndromic X-Linked Intellectual Disability 23 and Epidermolysis Bullosa, Junctional 1B, Severe . PDZD11 is involved in pathways related to the metabolism of water-soluble vitamins and cofactors, as well as the innate immune system .
Human recombinant PDZD11 refers to the protein produced through recombinant DNA technology, which involves inserting the gene encoding PDZD11 into a suitable expression system to produce the protein in a laboratory setting. This technology allows for the production of large quantities of the protein for research and therapeutic purposes.
Research on PDZD11 and other PDZ domain-containing proteins has provided significant insights into their roles in cellular and biological processes. Understanding the specificity, selectivity, and regulatory mechanisms of PDZ-mediated interactions can offer important insights into cell proliferation, cell polarity, and the formation and function of signal transduction complexes .