CRIPT Human

Cysteine-Rich PDZ-Binding Protein (CRPBP) is a recombinant human protein that plays a significant role in various cellular processes. This protein is characterized by the presence of cysteine-rich domains and PDZ-binding motifs, which are crucial for its interaction with other proteins and cellular components.

CRPBP contains multiple cysteine residues that form disulfide bonds, contributing to the protein’s stability and structural integrity. The PDZ-binding motifs in CRPBP allow it to interact with PDZ domains, which are common structural domains found in signaling proteins across various species, including bacteria, yeast, plants, viruses, and animals . PDZ domains are known for their role in anchoring receptor proteins in the membrane to cytoskeletal components, thereby organizing signaling complexes at cellular membranes .

The interaction between CRPBP and PDZ domains is essential for several biological processes, including:

• Signal Transduction: CRPBP is involved in the formation and function of signal transduction complexes, which are crucial for transmitting signals from the cell surface to the interior .
• Cell Polarity and Proliferation: PDZ domain-containing proteins, including those that interact with CRPBP, regulate cell polarity and proliferation, which are vital for maintaining tissue architecture and function .
• Transport and Ion Channel Signaling: CRPBP plays a role in the regulation of transport and ion channel signaling, contributing to the proper functioning of cellular processes .

Recent studies have utilized proteomic arrays and peptide libraries to investigate the binding properties of PDZ-mediated interactions involving CRPBP . These studies have provided insights into the specificity and regulatory mechanisms of these interactions, which are essential for understanding various cellular and biological processes .