A5101932813- Hereditary Neurological Disorders
- Lipid Membrane Structure and Behavior
- RNA Research and Splicing
- Neurological diseases and metabolism
- Molecular Sensors and Ion Detection
- Force Microscopy Techniques and Applications
- Supramolecular Self-Assembly in Materials
- Nanoparticle-Based Drug Delivery
- Enzyme Structure and Function
- Toxin Mechanisms and Immunotoxins
- Advanced NMR Techniques and Applications
Tampere University
2015-2020
Abstract Charcot-Marie-Tooth (CMT) disease is one of the most common inherited neuropathies. Recently, three CMT1-associated point mutations (I43N, T51P, and I52T) were discovered in abundant peripheral myelin protein P2. These trigger abnormal structure, leading to reduced nerve conduction velocity, muscle weakness, distal limb atrophy. P2 a myelin-specific expressed by Schwann cells that binds fatty acids membranes, contributing lipid homeostasis. We studied molecular basis patient...
Myelin is a multilayered proteolipid sheath wrapped around selected axons in the nervous system. Its constituent proteins play major roles forming of highly regular membrane structure. P2 myelin-specific protein fatty acid binding (FABP) superfamily, which able to stack lipid bilayers together, and it target for mutations human inherited neuropathy Charcot-Marie-Tooth disease. A conserved residue that has been proposed participate conformational changes FABPs Phe57. This thought be...
Myelin protein P2 is a peripheral membrane of the fatty acid-binding family that functions in formation and maintenance nerve myelin sheath. Several gene mutations cause human Charcot-Marie-Tooth neuropathy, but mature sheath assembly mechanism unclear. Here, cryo-EM myelin-like proteolipid multilayers revealed an ordered three-dimensional (3D) lattice molecules between stacked lipid bilayers, visualizing supramolecular at major dense line. The data disclosed single layer inserted two...
Myelin protein P2 is a fatty acid-binding structural component of the myelin sheath in peripheral nervous system, and its function related to membrane binding capacity. Here, link between dynamics structure was studied using elastic incoherent neutron scattering (EINS). The P38G mutation, at hinge β barrel α-helical lid, increased lipid stacking capacity human vitro, mutated also functional cultured cells. mutation did not change overall protein. For deeper insight into structure-function...
Abstract Myelin protein P2 is a peripheral membrane of the fatty acid binding family. It functions in formation and maintenance nerve myelin sheath, several mutations causing human Charot-Marie-Tooth neuropathy have been reported. Here, electron cryomicroscopy myelin-like proteolipid multilayers revealed three-dimensionally ordered lattice molecules between stacked lipid bilayers, visualizing its possible assembly at major dense line. A single layer inserted two bilayers tight intermembrane...