Legume lectin of view of protein structure. Despite the conserved structure of the legume lectin subunit, they can adopt a wide range of quaternary structures. The reason behind this remarkable variability is probably to be found in the interaction with multivalent ligands. Legume lectin The legume lectins (or L-type lectins) are a family of sugar-binding proteins or lectins found in the seeds and, in smaller amounts, in the roots, stems, leaves and bark of plants belonging to the Fabaceae family. The exact function of the legume lectins "in vivo" is unknown but they are probably involved in the defense of plants against
Myosin showed that it is plus-end directed. The movement mechanism for this myosin is poorly understood. Myosin X is an unconventional myosin motor, which is functional as a dimer. The dimerization of myosin X is thought to be antiparallel. This behavior has not been observed in other myosins. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments. Some research suggests it preferentially walks on bundles of actin, rather than single filaments. It is the first myosin motor found to exhibit this behavior. Myosin XI directs the movement of organelles such