GBP7 inhibitors are a class of chemical compounds that specifically target the GTP-binding protein 7 (GBP7), a member of the larger guanylate-binding proteins (GBPs) family. GBPs are part of the dynamin superfamily of large GTPases and play roles in a variety of cellular processes, including the modulation of immune responses and signaling pathways. GBP7 is involved in intracellular signaling, immune regulation, and potentially other cellular functions, given its ability to bind and hydrolyze GTP, a critical molecular activity in cellular signaling pathways. Inhibitors of GBP7 are designed to interfere with its GTPase activity, thus altering the protein's function in signaling cascades and cellular responses. The exact structure-activity relationships (SAR) of GBP7 inhibitors vary, but they often include functional groups that facilitate binding to the active or regulatory sites of the protein, blocking GTP hydrolysis or disrupting protein-protein interactions.
These inhibitors can be characterized by their ability to interact selectively with GBP7, which is achieved through the design of molecules that fit into its unique GTP-binding pocket or other functionally relevant domains. Structural studies of GBP7 have informed the development of inhibitors that exhibit high specificity and potency, minimizing off-target effects on other GTPases. GBP7 inhibitors can be categorized based on their mechanism of inhibition, whether they are competitive, non-competitive, or allosteric in nature. The development and characterization of these compounds provide important tools for studying the molecular and biochemical pathways in which GBP7 is involved, offering insights into its role in cellular processes and its interactions with other signaling molecules. Research on GBP7 inhibitors focuses on understanding the detailed structure-function relationship of the GTPase and the biochemical pathways it influences, contributing to a broader understanding of GBP family proteins and their regulation in cells.
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