C-type lectin The "NK Cell lectin-like receptors" are a very closely related group: Additional proteins containing this domain include: C-type lectin A C-type lectin (CLEC) is a type of carbohydrate-binding protein domain known as a lectin. The C-type designation is from their requirement for calcium for binding. Proteins that contain C-type lectin domains have a diverse range of functions including cell-cell adhesion, immune response to pathogens and apoptosis. Drickamer "et al." classified C-type lectins into 7 subgroups (I to VII) based on the order of the various protein domains in each protein. This classification was subsequently updated in 2002, leading to seven
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