fourtransmembrane

Four-transmembrane is a class of integral membrane proteins that have four transmembrane domains. These proteins are also known as 4TM proteins. They are characterized by their Specifically, they are predicted to cross the membrane four times using standard sequence analysis tools into the cytoplasm or the outer surface of the cell.

The four-transmembrane structure is a common feature of many transporters, receptors, and channels that are embedded in the plasma membrane. The transmembrane domains are usually hydrophobic regions of the protein that are capable of traversing the cell membrane, which consists of a phospholipid bilayer. The transmembrane domains can be aligned in a variety of topologies depending on the protein and the type of function it performs.

In general, the four-transmembrane structure is thought to provide a stable lipid-exposed surface for membrane binding and activation. The four-transmembrane domains also create a pore or cleft in the interior of the protein, where the transport function or signaling event occurs. Proteins in this class are involved in a wide range of processes, including sensing neurotransmitters, controlling synaptic function, and modifying protein signaling pathways.

Examples of four-transmembrane proteins include EGF receptors, G protein-coupled receptors (GPCRs), and other membrane receptors that have specific functions in cell to cell interaction. Bioinformatic analyses have categorized many novel membrane proteins with four-transmembrane topology using predictive models. These discoveries have led to broader annotation and structural insights that reflect diversity in both topology and function within the transmembrane space.