PDZK1 Human

PDZ domains typically consist of 80-90 amino acids forming 5-6 β-strands and 2-3 α-helices . They are involved in anchoring receptor proteins in the membrane to cytoskeletal components, thus organizing signaling complexes at cellular membranes . This structural arrangement allows PDZ domains to bind to the C-terminal sequences of their target proteins through a mechanism known as beta sheet augmentation .

PDZ domains are abundant in various species, including bacteria, yeast, plants, viruses, and animals . They regulate multiple biological processes such as transport, ion channel signaling, and other signal transduction systems . In humans, PDZ domain-containing proteins are involved in critical functions like cell proliferation, cell polarity, and the formation of signal transduction complexes .

PDZ Domain Containing 1 (PDZK1) is a specific protein that contains PDZ domains. It is known for its role in the regulation of various transporters and channels. PDZK1 interacts with several membrane proteins, including ion channels and transporters, thereby influencing their localization and function .

Human recombinant PDZK1 is a laboratory-produced version of the naturally occurring PDZK1 protein. Recombinant proteins are typically produced using techniques such as gene cloning and expression in host cells like bacteria or yeast. These recombinant proteins are used in research to study protein-protein interactions, signaling pathways, and potential therapeutic targets.

The study of PDZ domains and their interactions has been greatly enhanced by proteomic methods such as large-scale protein arrays and peptide libraries . These methods have provided insights into the binding properties and regulatory mechanisms of PDZ-mediated interactions, which are essential for understanding many cellular and biological processes .