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Membrane proteins are frequently significant pharmacological therapeutic targets and serve critical roles in cellular processes. Lipid membranes contain integral membrane proteins (IMPs). In sequenced genomes, between 15 and 30 percent of open reading frames are thought to code for membrane proteins. This protein complex participates in cell signaling and motility as well as a number of other critical tasks that are essential to the health of the cell, including the controlled flow of molecules, nutrients, and ions across lipid bilayers. This dependence on membrane proteins as medication targets is expected given that over 60% of medicines used today target IMPs to achieve their therapeutic action.
Latest Research and Reviews
Membrane proteins can be found on intracellular organelles or at the surface of cell membranes. Ion channels and receptors are examples of integral membrane proteins that traverse the membrane. A fatty acid, prenyl group, glycophosphatidylinositol (GPI), or hydrophobic protein patch acts as an anchor to bind peripheral membrane proteins, such as certain signaling proteins, to the cell membrane.
| Paper Title | Structural basis of organic cation transporter-3 inhibition |
| Journal | Nature Communications |
| Published | 2022 |
| Description | Catecholamines, medications, and xenobiotics are more easily transported through plasma membranes in a variety of tissues throughout the human body thanks to organic cation transporters (OCTs). Most tissues, including the heart, brain, and liver, absorb monoamines with low affinities and high capacities thanks in large part to OCT3. Its dysregulation contributes to illnesses. Here, they describe the 3.2-resolution cryo-EM structure of human OCT3. |
| Paper Title | An active site loop toggles between conformations to control antibiotic hydrolysis and inhibition potency for CTX-M β-lactamase drug-resistance enzymes |
| Journal | Nature Communications |
| Published | 2022 |
| Description | Drug resistance results from β-lactamases inactivating β-lactam antibiotics. As a result, β-lactamase inhibitors, such as the naturally occurring β-lactamase inhibitory protein (BLIP), can overcome this resistance. The common β-lactamases CTX-M-14 and CTX-M-15 share an 83% sequence similarity. This study demonstrates that BLIP potently inhibits CTX-M-15 while only moderately inhibiting CTX-M-14. |
References
- Khanppnavar, B.; et al. Structural basis of organic cation transporter-3 inhibition. Nature Communications. 2022, 13: 6714.
- Lu, S.; et al. An active site loop toggles between conformations to control antibiotic hydrolysis and inhibition potency for CTX-M β-lactamase drug-resistance enzymes. Nature Communications. 2022, 13: 6726.
