Scientists Solve Structure of Protein That Powers Cell Movement
News Sep 23, 2005
The Proceedings of the National Academy of Science has published the three-dimensional structure of a key part of the molecular motor protein, myosin V.
The structure, which describes a protein responsible for the movement of the inner workings of our cells, was determined by a collaborative team of scientists led by Dr. Roberto Dominguez at the not-for-profit Boston Biomedical Research Institute, including Drs. Zenon Grabarek and Renne Lu.
Few people would argue that motility, or movement is one of the most characteristic and fundamental attributes of life. The flexing of a muscle, a heartbeat, digestion, or the much more subtle but immensely important transport that takes place within our cells, are all processes that are different expressions of motility and have one thing in common. All are powered by the protein myosin, or more strictly speaking, by one of the members of the myosin family of molecular motor proteins.
The scientists at Boston Biomedical combined the power of several techniques including X-ray crystallography, resonance energy transfer and molecular modeling to obtain a three-dimensional, atomic resolution structure of the neck region of myosin V. This form of myosin is responsible for organelle transport inside the cells.
The neck region was initially thought to be a mere link within the molecule. The scientists at Boston Biomedical have demonstrated that the myosin's neck region has an unexpectedly complex structure, demonstrating that in addition to the previously recognized function as a rigid link, it is also involved in regulation of function of this important protein and possibly mediates its interactions with other proteins. Understanding the function of myosin V could shed light on disease states involving inappropriate cell movement, such as cancer metastasis.
Boston Biomedical Research Institute is a not-for-profit institution dedicated to the understanding, treatment and prevention of specific human diseases including cancer, Alzheimer's disease, muscular dystrophy, diabetes and conditions such as obesity and reproductive health problems.
Chinese researchers have developed interfacially polymerized porous polymer particles for low- abundance glycopeptide separation. These polymer particles - with hydrophilic-hydrophobic heterostructured nanopores - can separate low-abundance glycopeptides from complex biological samples with high-abundance background molecules efficiently.