Extracellular signalling molecules that bind to Enzyme-linked receptors are converted by monomeric g-proteins while it is not shown by heterotrimeric g-proteins. In this way, the function of monomeric g-proteins differs from that of heterotrimeric g-proteins.
What is the functional difference between Monomeric g-proteins and heterotrimeric g-proteins?
- Guanosine triphosphate (GTP) and guanosine diphosphate can be bound by g-proteins, which are specialized proteins (GDP). Some G proteins are tiny proteins with a single component, such as the signalling protein Ras.
- These g-proteins are of two types: monomeric and heterotrimeric g-proteins that differ from each other in terms of structure as well as functions. Monomeric G protein is a small membrane-associated G protein made up of only an alpha subunit, whereas heteromeric G protein is a large membrane-associated G protein composed of alpha, beta, and gamma subunits.
- These differ from each other in terms of function: Monomeric G-proteins transform extracellular signalling chemicals that attach to enzyme-linked receptors. Trimeric G-proteins transform extracellular signalling chemicals that attach to G-protein-related receptors.
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